Reviewed, UniProtKB/Swiss-Prot P11411 (G6PD_LEUME)

Names and origin

Protein names

Recommended name:
    Glucose-6-phosphate 1-dehydrogenase
      Short name=G6PD
    EC=1.1.1.49

Gene names

Name:

zwf

Organism

Leuconostoc mesenteroides

Taxonomic identifier

1245 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Leuconostoc

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH.
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro glucose-6-phosphate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 486

485

Glucose-6-phosphate 1-dehydrogenase

PRO_0000068125

Sites

Active site

241

1

Proton acceptor

Binding site

15

1

NADP

Binding site

47

1

NADP

Binding site

179

1

Substrate

Binding site

183

1

Substrate

Binding site

344

1

Substrate

Experimental info

Mutagenesis

22

1

K → Q: Decreases KM for substrate over 30-fold. Ref.4

Mutagenesis

47

1

R → A: Strongly reduces affinity for NADP. Ref.4

Mutagenesis

178

1

D → N: Decreases Kcat over 100-fold. Ref.6

Mutagenesis

179

1

H → N: Decreases KM for substrate over 200-fold. Ref.6

Mutagenesis

183

1

K → Q: Decreases KM for substrate 1000-fold. Ref.4

Mutagenesis

241

1

H → N: Decreases Kcat over 10000-fold. Ref.6

Mutagenesis

344

1

K → Q: Decreases KM for substrate over 300-fold. Ref.4

Sequence conflict

154 – 156

3

SYD → HYI AA sequence Ref.2

Sequence conflict

165

1

L → F AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

486

Helix Strand Turn

Details...

Beta strand

7 – 12

6

Turn

13 – 15

3

Helix

17 – 21

5

Helix

23 – 32

10

Beta strand

38 – 48

11

Helix

52 – 63

12

Helix

64 – 66

3

Helix

70 – 77

8

Beta strand

80 – 84

5

Helix

92 – 106

15

Beta strand

113 – 117

5

Helix

121 – 123

3

Helix

124 – 133

10

Beta strand

139 – 141

3

Beta strand

143 – 147

5

Helix

155 – 165

11

Turn

166 – 168

3

Helix

171 – 173

3

Beta strand

174 – 176

3

Helix

179 – 182

4

Helix

184 – 188

5

Helix

189 – 194

6

Helix

197 – 200

4

Turn

205 – 207

3

Beta strand

208 – 216

9

Helix

225 – 236

12

Turn

237 – 240

4

Helix

241 – 250

10

Beta strand

255 – 258

4

Helix

259 – 270

12

Helix

278 – 284

7

Beta strand

285 – 290

6

Helix

301 – 303

3

Beta strand

315 – 321

7

Helix

326 – 328

3

Beta strand

333 – 343

11

Beta strand

345 – 352

8

Beta strand

361 – 363

3

Beta strand

369 – 377

9

Beta strand

379 – 387

9

Beta strand

389 – 392

4

Beta strand

395 – 403

9

Helix

406 – 411

6

Helix

415 – 425

11

Helix

434 – 452

19

Beta strand

459 – 461

3

Beta strand

465 – 467

3

Helix

469 – 476

8

Turn

477 – 479

3

Sequences

	Sequence		Length	Mass (Da)
	P11411-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: AA43433F83ED091D	FASTA	486	54,441
	10 20 30 40 50 60 MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL NDDEFKQLVR 70 80 90 100 110 120 DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA 130 140 150 160 170 180 PRFFGTIAKY LKSEGLLADT GYNRLMIEKP FGTSYDTAAE LQNDLENAFD DNQLFRIDHY 190 200 210 220 230 240 LGKEMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN 250 260 270 280 290 300 HTMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP 310 320 330 340 350 360 YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI VFKAGTFNFG 370 380 390 400 410 420 SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEPYERMI 430 440 450 460 470 480 HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG

References

[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: 2071589] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 3100332] [Abstract] Cited for: PROTEIN SEQUENCE OF 147-188.
[3]	"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: 1304341] [Abstract] Cited for: IMPORTANCE OF LYS-22 FOR SUBSTRATE-BINDING.
[4]	"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: 11106479] [Abstract] Cited for: MUTAGENESIS OF LYS-22; ARG-47; LYS-183 AND LYS-344.
[5]	"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: 7881907] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[6]	"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: 9485426] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-241, MUTAGENESIS OF ASP-178; HIS-179 AND HIS-241.
[7]	"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: 11106478] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS ASN-178 AND CYS-366 IN COMPLEX WITH NAD; NADP AND SUBSTRATE.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M64446 Genomic DNA. Translation: AAA25265.1.

PIR

A39864.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-485	[»]
1H94	X-ray	2.50	A	2-485	[»]
1H9A	X-ray	2.16	A	2-485	[»]
1H9B	X-ray	2.40	A	2-485	[»]
2DPG	X-ray	2.50	A	2-486	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13060.

BRENDA

1.1.1.49. 703.

Family and domain databases

InterPro

IPR001282. Glc-6-P_DH.
IPR019796. Glc-6-P_DH_AS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR23429. G6PDH. 1 hit.

Pfam

PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000110. G6PD. 1 hit.

PRINTS

PR00079. G6PDHDRGNASE.

TIGRFAMs

TIGR00871. zwf. 1 hit.

PROSITE

PS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

G6PD_LEUME

Accession

Primary (citable) accession number: P11411

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 92 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)