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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: pentose phosphate pathway

    This protein is involved in step 1 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Glucose-6-phosphate 1-dehydrogenase (zwf)
    2. no protein annotated in this organism
    3. no protein annotated in this organism
    This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei47NADPUniRule annotation3 Publications1
    Binding sitei149NADPUniRule annotation1 Publication1
    Binding sitei179Substrate1 Publication1
    Binding sitei183Substrate1 Publication1
    Binding sitei217Substrate1 Publication1
    Binding sitei236Substrate1 Publication1
    Active sitei241Proton acceptorUniRule annotation1 Publication1
    Binding sitei339Substrate1 Publication1
    Binding sitei344Substrate1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi13 – 20NADPUniRule annotation3 Publications8
    Nucleotide bindingi86 – 87NADPUniRule annotation3 Publications2

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi15T → A: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi15T → S: Decreases catalytic efficiency toward glucose 6-phosphate (with NAD). 1 Publication1
    Mutagenesisi22K → E: Almost loss of activity. 2 Publications1
    Mutagenesisi22K → Q: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 2 Publications1
    Mutagenesisi22K → R: Decreases catalytic efficiency toward glucose 6-phosphate. 2 Publications1
    Mutagenesisi47R → A: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi48Q → A or E: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi150P → G or V: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi178D → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi179H → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi180Y → F: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi183K → Q or R: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi241H → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi344K → Q or R: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi375D → Q: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1
    Mutagenesisi416Y → F: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL1741173.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00000681252 – 486Glucose-6-phosphate 1-dehydrogenaseAdd BLAST485

    Proteomic databases

    PRIDEiP11411.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Chemistry databases

    BindingDBiP11411.

    Structurei

    Secondary structure

    1486
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 12Combined sources6
    Turni13 – 15Combined sources3
    Helixi17 – 21Combined sources5
    Helixi23 – 32Combined sources10
    Beta strandi38 – 48Combined sources11
    Helixi52 – 63Combined sources12
    Helixi64 – 66Combined sources3
    Helixi70 – 77Combined sources8
    Beta strandi80 – 84Combined sources5
    Helixi92 – 106Combined sources15
    Beta strandi113 – 117Combined sources5
    Helixi121 – 123Combined sources3
    Helixi124 – 133Combined sources10
    Beta strandi139 – 141Combined sources3
    Beta strandi143 – 147Combined sources5
    Helixi155 – 165Combined sources11
    Turni166 – 168Combined sources3
    Helixi171 – 173Combined sources3
    Beta strandi174 – 176Combined sources3
    Helixi179 – 182Combined sources4
    Helixi184 – 188Combined sources5
    Helixi189 – 194Combined sources6
    Helixi197 – 200Combined sources4
    Turni205 – 207Combined sources3
    Beta strandi208 – 216Combined sources9
    Helixi222 – 224Combined sources3
    Helixi225 – 236Combined sources12
    Turni237 – 240Combined sources4
    Helixi241 – 250Combined sources10
    Beta strandi255 – 258Combined sources4
    Helixi259 – 270Combined sources12
    Helixi278 – 284Combined sources7
    Beta strandi285 – 290Combined sources6
    Beta strandi294 – 298Combined sources5
    Helixi301 – 303Combined sources3
    Beta strandi315 – 321Combined sources7
    Helixi326 – 328Combined sources3
    Beta strandi333 – 343Combined sources11
    Beta strandi345 – 352Combined sources8
    Beta strandi361 – 363Combined sources3
    Beta strandi369 – 377Combined sources9
    Beta strandi379 – 387Combined sources9
    Beta strandi389 – 392Combined sources4
    Beta strandi395 – 403Combined sources9
    Helixi406 – 411Combined sources6
    Helixi415 – 425Combined sources11
    Helixi428 – 430Combined sources3
    Helixi434 – 452Combined sources19
    Beta strandi459 – 461Combined sources3
    Beta strandi465 – 467Combined sources3
    Helixi469 – 476Combined sources8
    Turni477 – 479Combined sources3

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP11411.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK00036.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00966. G6PD. 1 hit.
    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.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti154 – 156SYD → HYI AA sequence (PubMed:3100332).Curated3
    Sequence conflicti165L → F AA sequence (PubMed:3100332).Curated1

    Sequence databases

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

    Genome annotation databases

    KEGGiag:AAA25265.

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP11411.
    ChEMBLiCHEMBL1741173.

    Proteomic databases

    PRIDEiP11411.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAA25265.

    Phylogenomic databases

    KOiK00036.

    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. 1 hit.
    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.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00871. zwf. 1 hit.
    PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 129 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

    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 one 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.