Reviewed, UniProtKB/Swiss-Prot O24357 (G6PDC_SPIOL)

Names and origin

Protein names

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

Gene names

Name:

G6PD

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are involved in membrane synthesis and cell division. May be involved in nitrite reduction.
Catalytic activity	D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH.
Enzyme regulation	Regulated by metabolites. Post-translationally inactivated by cysteine-mediated redox modification via the ferredoxin-thioredoxin system in the light and this avoids futile cycles with photosynthetic CO2 fixation By similarity.
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subunit structure	Homodimer By similarity.
Subcellular location	Plastid › chloroplast By similarity.
Sequence similarities	Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 574		Glucose-6-phosphate 1-dehydrogenase, chloroplastic		PRO_0000010439
Sites
	Active site	322	1	Proton acceptor By similarity
	Binding site	95	1	NADP By similarity
	Binding site	127	1	NADP By similarity
	Binding site	260	1	Substrate By similarity
	Binding site	264	1	Substrate By similarity
	Binding site	423	1	Substrate By similarity
Amino acid modifications
	Disulfide bond	145 ↔ 153		Redox modulation By similarity

Sequences

	Sequence		Length	Mass (Da)
	O24357-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: D498DB32D25849AA	FASTA	574	65,180
	10 20 30 40 50 60 MEELVSCHHL PLLCLQSSVP PNGCLTFFQD SACQRCSHSE FSNGHPLNDV SLQNDVAVNP 70 80 90 100 110 120 IVAKSIDPSA DLQLLPLLES VKEEPTLSII VVGASGDLAK KKIFPALFAL FYENCLPENF 130 140 150 160 170 180 TVFGFSRTEM NDEELRTMIS KTLTCRIDQR ENCGEKMDHF LQRCFYHSGQ YNSEDDFSGL 190 200 210 220 230 240 DCKLKEKEAG RLQNRLFYLS IPPNIFVDVV RCVSHRASSA SGWTRVIVEK PFGRDSDSSR 250 260 270 280 290 300 ELTRSFKQYL SEDQIFRIDH YLGKELVENL SVLRFSNLVF EPLWSRNYIR NVQLIFSEDF 310 320 330 340 350 360 GTEGRGGYFD NYGIIRDIMQ NHLLQILALF AMETPVSLDA EDIRNEKVKV LRSMKPLKLQ 370 380 390 400 410 420 DVVVGQYKGH SKGNKSYSGY TDDPTVPNNS VTPTFAAAAL FIDNARWDGV PFLMKAGKAL 430 440 450 460 470 480 HTKRAEIRVQ FRHVPGNLYK KTFGTDLDKA TNELVLRVQP DEAIYLKINN KVPGLGMRLD 490 500 510 520 530 540 RTDLNLCYST RYRGEIPDAY ERLLLDAIEG ERRLFIRSDK LDAAWSLFTP LLKELEEKKV 550 560 570 APELYPYGSR GPVGAHYLAA KHNVRWGDLS GEDS

References

[1]	Fink A., Diogon T., Perroud P.F., Crespi P., Greppin H. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Matador. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ000182 mRNA. Translation: CAA03939.1.
PIR	T09088.
3D structure databases
SMR	O24357. Positions 82-568.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.49. 286.
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

G6PDC_SPIOL

Accession

Primary (citable) accession number: O24357

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)