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Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.363) (Glucose-6-phosphate dehydrogenase (NAD(P)( )))

 G6PD_LEUME              Reviewed;         486 AA.
P11411;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 134.
RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966};
Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
EC=1.1.1.363 {ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11106479, ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688, ECO:0000269|PubMed:9485426};
AltName: Full=Glucose-6-phosphate dehydrogenase (NAD(P)(+)) {ECO:0000305};
Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966};
Leuconostoc mesenteroides.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae;
Leuconostoc.
NCBI_TaxID=1245;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 12291;
PubMed=2071589;
Lee W.T., Flynn T.G., Lyons C., Levy H.R.;
"Cloning of the gene and amino acid sequence for glucose 6-phosphate
dehydrogenase from Leuconostoc mesenteroides.";
J. Biol. Chem. 266:13028-13034(1991).
[2]
PROTEIN SEQUENCE OF 147-188.
PubMed=3100332; DOI=10.1016/0014-5793(87)81445-X;
Bhadbhade M.M., Adams M.J., Flynn T.G., Levy H.R.;
"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.";
FEBS Lett. 211:243-246(1987).
[3]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=4396688;
Olive C., Geroch M.E., Levy H.R.;
"Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides.
Kinetic studies.";
J. Biol. Chem. 246:2047-2057(1971).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-22.
PubMed=1304341; DOI=10.1002/pro.5560010304;
Lee W.T., Levy H.R.;
"Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate
dehydrogenase participates in substrate binding through charge-charge
interaction.";
Protein Sci. 1:329-334(1992).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-15; LYS-22;
ARG-47; GLN-48; PRO-150; TYR-180; LYS-183; LYS-344; ASP-375 AND
TYR-416.
PubMed=11106479; DOI=10.1021/bi0014610;
Vought V., Ciccone T., Davino M.H., Fairbairn L., Lin Y.,
Cosgrove M.S., Adams M.J., Levy H.R.;
"Delineation of the roles of amino acids involved in the catalytic
functions of Leuconostoc mesenteroides glucose 6-phosphate
dehydrogenase.";
Biochemistry 39:15012-15021(2000).
[6] {ECO:0000244|PDB:1DPG}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=7881907; DOI=10.1016/S0969-2126(94)00110-3;
Rowland P., Basak A.K., Gover S., Levy H.R., Adams M.J.;
"The three-dimensional structure of glucose 6-phosphate dehydrogenase
from Leuconostoc mesenteroides refined at 2.0-A resolution.";
Structure 2:1073-1087(1994).
[7] {ECO:0000244|PDB:2DPG}
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-241 IN COMPLEX
WITH NADP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF ASP-178; HIS-179 AND
HIS-241.
PubMed=9485426; DOI=10.1021/bi972069y;
Cosgrove M.S., Naylor C., Paludan S., Adams M.J., Levy H.R.;
"On the mechanism of the reaction catalyzed by glucose 6-phosphate
dehydrogenase.";
Biochemistry 37:2759-2767(1998).
[8] {ECO:0000244|PDB:1E77, ECO:0000244|PDB:1E7M, ECO:0000244|PDB:1E7Y}
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, AND SUBUNIT.
PubMed=11106478; DOI=10.1021/bi0014608;
Cosgrove M.S., Gover S., Naylor C.E., Vandeputte-Rutten L.,
Adams M.J., Levy H.R.;
"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.";
Biochemistry 39:15002-15011(2000).
[9] {ECO:0000244|PDB:1H93, ECO:0000244|PDB:1H94, ECO:0000244|PDB:1H9A, ECO:0000244|PDB:1H9B}
X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) IN COMPLEXES WITH NAD AND NADP.
PubMed=11320304; DOI=10.1107/S0907444901003420;
Naylor C.E., Gover S., Basak A.K., Cosgrove M.S., Levy H.R.,
Adams M.J.;
"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.";
Acta Crystallogr. D 57:635-648(2001).
-!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
phosphogluconolactone. Can utilize either NADP(+) or NAD(+).
{ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106479,
ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688,
ECO:0000269|PubMed:9485426}.
-!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NAD(P)(+) = 6-phospho-
D-glucono-1,5-lactone + NAD(P)H. {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11106479, ECO:0000269|PubMed:1304341,
ECO:0000269|PubMed:4396688, ECO:0000269|PubMed:9485426}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=114 uM for glucose 6-phosphate (with NADP)
{ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426};
KM=69 uM for glucose 6-phosphate (with NAD)
{ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426};
KM=8.0 uM for NADP {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:9485426};
KM=160 uM for NAD {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:9485426};
pH dependence:
Optimum pH is 5.4-8.9. {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:9485426};
-!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
step 1/3. {ECO:0000255|HAMAP-Rule:MF_00966}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:9485426}.
-!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
family. {ECO:0000255|HAMAP-Rule:MF_00966}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/ZF/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M64446; AAA25265.1; -; Genomic_DNA.
PIR; A39864; A39864.
PDB; 1DPG; X-ray; 2.00 A; A/B=2-486.
PDB; 1E77; X-ray; 2.69 A; A=2-486.
PDB; 1E7M; X-ray; 2.54 A; A=2-486.
PDB; 1E7Y; X-ray; 2.48 A; A=2-486.
PDB; 1H93; X-ray; 2.20 A; A=2-486.
PDB; 1H94; X-ray; 2.50 A; A=2-486.
PDB; 1H9A; X-ray; 2.16 A; A=2-486.
PDB; 1H9B; X-ray; 2.40 A; A=2-486.
PDB; 2DPG; X-ray; 2.50 A; A=2-486.
PDBsum; 1DPG; -.
PDBsum; 1E77; -.
PDBsum; 1E7M; -.
PDBsum; 1E7Y; -.
PDBsum; 1H93; -.
PDBsum; 1H94; -.
PDBsum; 1H9A; -.
PDBsum; 1H9B; -.
PDBsum; 2DPG; -.
ProteinModelPortal; P11411; -.
SMR; P11411; -.
BindingDB; P11411; -.
ChEMBL; CHEMBL1741173; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB04122; beta-D-glucose 6-phosphate.
DrugBank; DB02338; Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate.
PRIDE; P11411; -.
KEGG; ag:AAA25265; -.
KO; K00036; -.
BioCyc; MetaCyc:MONOMER-13060; -.
BRENDA; 1.1.1.363; 839.
SABIO-RK; P11411; -.
UniPathway; UPA00115; UER00408.
EvolutionaryTrace; P11411; -.
GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
HAMAP; MF_00966; G6PD; 1.
InterPro; IPR001282; G6P_DH.
InterPro; IPR019796; G6P_DH_AS.
InterPro; IPR022675; G6P_DH_C.
InterPro; IPR022674; G6P_DH_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR23429; PTHR23429; 1.
Pfam; PF02781; G6PD_C; 1.
Pfam; PF00479; G6PD_N; 1.
PIRSF; PIRSF000110; G6PD; 1.
PRINTS; PR00079; G6PDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00871; zwf; 1.
PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Direct protein sequencing;
Glucose metabolism; NAD; NADP; Oxidoreductase.
INIT_MET 1 1 Removed.
CHAIN 2 486 Glucose-6-phosphate 1-dehydrogenase.
/FTId=PRO_0000068125.
NP_BIND 13 20 NADP. {ECO:0000255|HAMAP-Rule:MF_00966,
ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11320304,
ECO:0000269|PubMed:9485426}.
NP_BIND 86 87 NADP. {ECO:0000255|HAMAP-Rule:MF_00966,
ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11320304,
ECO:0000269|PubMed:9485426}.
ACT_SITE 241 241 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00966,
ECO:0000269|PubMed:9485426}.
BINDING 47 47 NADP. {ECO:0000255|HAMAP-Rule:MF_00966,
ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11320304,
ECO:0000269|PubMed:9485426}.
BINDING 149 149 NADP. {ECO:0000255|HAMAP-Rule:MF_00966,
ECO:0000269|PubMed:11320304}.
BINDING 179 179 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 183 183 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 217 217 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 236 236 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 339 339 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 344 344 Substrate. {ECO:0000305|PubMed:11106478}.
MUTAGEN 15 15 T->A: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 15 15 T->S: Decreases catalytic efficiency
toward glucose 6-phosphate (with NAD).
{ECO:0000269|PubMed:11106479}.
MUTAGEN 22 22 K->E: Almost loss of activity.
{ECO:0000269|PubMed:11106479,
ECO:0000269|PubMed:1304341}.
MUTAGEN 22 22 K->Q: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479,
ECO:0000269|PubMed:1304341}.
MUTAGEN 22 22 K->R: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479,
ECO:0000269|PubMed:1304341}.
MUTAGEN 47 47 R->A: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 48 48 Q->A,E: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 150 150 P->G,V: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 178 178 D->N: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:9485426}.
MUTAGEN 179 179 H->N: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:9485426}.
MUTAGEN 180 180 Y->F: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 183 183 K->Q,R: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 241 241 H->N: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:9485426}.
MUTAGEN 344 344 K->Q,R: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 375 375 D->Q: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 416 416 Y->F: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
CONFLICT 154 156 SYD -> HYI (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 165 165 L -> F (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 7 12 {ECO:0000244|PDB:1DPG}.
TURN 13 15 {ECO:0000244|PDB:1DPG}.
HELIX 17 21 {ECO:0000244|PDB:1DPG}.
HELIX 23 32 {ECO:0000244|PDB:1DPG}.
STRAND 38 48 {ECO:0000244|PDB:1DPG}.
HELIX 52 63 {ECO:0000244|PDB:1DPG}.
HELIX 64 66 {ECO:0000244|PDB:1DPG}.
HELIX 70 77 {ECO:0000244|PDB:1DPG}.
STRAND 80 84 {ECO:0000244|PDB:1DPG}.
HELIX 92 106 {ECO:0000244|PDB:1DPG}.
STRAND 113 117 {ECO:0000244|PDB:1DPG}.
HELIX 121 123 {ECO:0000244|PDB:1DPG}.
HELIX 124 133 {ECO:0000244|PDB:1DPG}.
STRAND 139 141 {ECO:0000244|PDB:1DPG}.
STRAND 143 147 {ECO:0000244|PDB:1DPG}.
HELIX 155 165 {ECO:0000244|PDB:1DPG}.
TURN 166 168 {ECO:0000244|PDB:1DPG}.
HELIX 171 173 {ECO:0000244|PDB:1DPG}.
STRAND 174 176 {ECO:0000244|PDB:1DPG}.
HELIX 179 182 {ECO:0000244|PDB:1DPG}.
HELIX 184 188 {ECO:0000244|PDB:1DPG}.
HELIX 189 194 {ECO:0000244|PDB:1DPG}.
HELIX 197 200 {ECO:0000244|PDB:1DPG}.
TURN 205 207 {ECO:0000244|PDB:1DPG}.
STRAND 208 216 {ECO:0000244|PDB:1DPG}.
HELIX 222 224 {ECO:0000244|PDB:1H9A}.
HELIX 225 236 {ECO:0000244|PDB:1DPG}.
TURN 237 240 {ECO:0000244|PDB:1DPG}.
HELIX 241 250 {ECO:0000244|PDB:1DPG}.
STRAND 255 258 {ECO:0000244|PDB:1DPG}.
HELIX 259 270 {ECO:0000244|PDB:1DPG}.
HELIX 278 284 {ECO:0000244|PDB:1DPG}.
STRAND 285 290 {ECO:0000244|PDB:1DPG}.
STRAND 294 298 {ECO:0000244|PDB:1H9A}.
HELIX 301 303 {ECO:0000244|PDB:1DPG}.
STRAND 315 321 {ECO:0000244|PDB:1DPG}.
HELIX 326 328 {ECO:0000244|PDB:1DPG}.
STRAND 333 343 {ECO:0000244|PDB:1DPG}.
STRAND 345 352 {ECO:0000244|PDB:1DPG}.
STRAND 361 363 {ECO:0000244|PDB:1DPG}.
STRAND 369 377 {ECO:0000244|PDB:1DPG}.
STRAND 379 387 {ECO:0000244|PDB:1DPG}.
STRAND 389 392 {ECO:0000244|PDB:1DPG}.
STRAND 395 403 {ECO:0000244|PDB:1DPG}.
HELIX 406 411 {ECO:0000244|PDB:1DPG}.
HELIX 415 425 {ECO:0000244|PDB:1DPG}.
HELIX 428 430 {ECO:0000244|PDB:1H94}.
HELIX 434 452 {ECO:0000244|PDB:1DPG}.
STRAND 459 461 {ECO:0000244|PDB:1DPG}.
STRAND 465 467 {ECO:0000244|PDB:1DPG}.
HELIX 469 476 {ECO:0000244|PDB:1DPG}.
TURN 477 479 {ECO:0000244|PDB:1DPG}.
SEQUENCE 486 AA; 54441 MW; AA43433F83ED091D CRC64;
MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL NDDEFKQLVR
DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA
PRFFGTIAKY LKSEGLLADT GYNRLMIEKP FGTSYDTAAE LQNDLENAFD DNQLFRIDHY
LGKEMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN
HTMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP
YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI VFKAGTFNFG
SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEPYERMI
HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD
AWVFKG


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