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P11411

- G6PD_LEUME

UniProt

P11411 - G6PD_LEUME

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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 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
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-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 .
PIRi A39864.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 116 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