Glucose-6-phosphate 1-dehydrogenase - Rattus norvegicus (Rat)

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P05370 (G6PD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:	G6pdx
Synonyms:	G6pd

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	515 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⁺ = 6-phospho-D-glucono-1,5-lactone + NADPH.
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Miscellaneous	Has NADP both as cofactor (bound to the N-terminal domain) and as structural element bound to the C-terminal domain.
Sequence similarities	Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to oxidative stress Inferred from electronic annotation. Source: Compara cholesterol biosynthetic process Inferred from electronic annotation. Source: Compara cytokine production Inferred from electronic annotation. Source: Compara erythrocyte maturation Inferred from electronic annotation. Source: Compara glucose 6-phosphate metabolic process Inferred from direct assay PubMed 17447164. Source: RGD glutathione metabolic process Inferred from electronic annotation. Source: Compara negative regulation of protein glutathionylation Inferred from electronic annotation. Source: Compara pentose biosynthetic process Inferred from electronic annotation. Source: Compara pentose-phosphate shunt, oxidative branch Inferred from mutant phenotype PubMed 9794092. Source: RGD regulation of neuron apoptotic process Inferred from direct assay PubMed 12414804. Source: RGD response to ethanol Inferred from direct assay PubMed 18488910. Source: RGD response to food Inferred from expression pattern PubMed 19076169. Source: RGD response to organic cyclic compound Inferred from expression pattern PubMed 17250641. Source: RGD ribose phosphate biosynthetic process Inferred from electronic annotation. Source: Compara
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 1834654. Source: RGD internal side of plasma membrane Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 15942958. Source: RGD
Molecular_function	NADP binding Inferred from direct assay PubMed 17447164. Source: RGD glucose binding Inferred from direct assay PubMed 17447164. Source: RGD glucose-6-phosphate dehydrogenase activity Inferred from direct assay PubMed 11735100 PubMed 17447164 PubMed 18062843 PubMed 1834654 PubMed 2843500. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 515

514

Glucose-6-phosphate 1-dehydrogenase

PRO_0000068087

Sites

Active site

263

Proton acceptor By similarity

Binding site

NADP By similarity

Binding site

NADP By similarity

Binding site

201

Substrate By similarity

Binding site

205

Substrate By similarity

Binding site

238

NADP By similarity

Binding site

357

NADP By similarity

Binding site

487

NADP By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.3

Modified residue

N6-acetyllysine By similarity

Modified residue

171

N6-acetyllysine By similarity

Modified residue

403

N6-acetyllysine By similarity

Modified residue

432

N6-acetyllysine By similarity

Modified residue

497

N6-acetyllysine By similarity

Experimental info

Sequence conflict

320

N → D AA sequence Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P05370 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8E92FFF3BF5A959B
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FASTA

515

59,376

        10         20         30         40         50         60 
MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL 

        70         80         90        100        110        120 
LPEDTFIVGY ARSRLTVDDI RKQSEPFFKV TPEERPKLEE FFARNSYVAG QYDDPASYKH 

       130        140        150        160        170        180 
LNSHMNALHQ GMQANRLFYL ALPPTVYEAV TKNIQEICMS QTGWNRIIVE KPFGRDLQSS 

       190        200        210        220        230        240 
NQLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP 

       250        260        270        280        290        300 
FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTD SDDVRDEKVK VLKCISEVET 

       310        320        330        340        350        360 
DNVVLGQYVG NPSGEGEATN GYLDDPTVPH GSTTATFAAA VLYVENERWD GVPFILRCGK 

       370        380        390        400        410        420 
ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL 

       430        440        450        460        470        480 
DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH KIDREKPQPI 

       490        500        510 
PYVYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence of a cDNA encoding rat glucose-6-phosphate dehydrogenase." Ho Y., Howard A.J., Crapo J.D. Nucleic Acids Res. 16:7746-7746(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[3]	"Glucose-6-phosphate dehydrogenase. Characteristics revealed by the rat liver enzyme structure." Jeffery J., Barros-Soederling J., Murray L., Wood I., Hansen R., Szepesi B., Joernvall H. Eur. J. Biochem. 186:551-556(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-514. Strain: Wistar. Tissue: Liver.
[4]	Fritz R.S., Kletzien R.F. Submitted (NOV-1989) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-515.
[5]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 58-72; 176-192 AND 228-257, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X07467 mRNA. Translation: CAA30355.1. BC081820 mRNA. Translation: AAH81820.1. M26655, M26653, M26654 Genomic DNA. Translation: AAA41179.1.
IPI	IPI00231637.
PIR	S01233.
RefSeq	NP_058702.1. NM_017006.2.
UniGene	Rn.11040.
3D structure databases
ProteinModelPortal	P05370.
SMR	P05370. Positions 28-515.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000053157.
PTM databases
PhosphoSite	P05370.
2D gel databases
World-2DPAGE	0004:P05370.
Proteomic databases
PaxDb	P05370.
PRIDE	P05370.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000056317; ENSRNOP00000053157; ENSRNOG00000037254.
GeneID	24377.
KEGG	rno:24377.
Organism-specific databases
CTD	2539.
RGD	2645. G6pdx.
Phylogenomic databases
eggNOG	COG0364.
GeneTree	ENSGT00530000063435.
HOGENOM	HOG000046192.
HOVERGEN	HBG000856.
InParanoid	P05370.
KO	K00036.
OrthoDB	EOG4VHK69.
Enzyme and pathway databases
SABIO-RK	P05370.
UniPathway	UPA00115; UER00408.
Gene expression databases
Genevestigator	P05370.
GermOnline	ENSRNOG00000037254. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR001282. G6P_DH. IPR019796. G6P_DH_AS. IPR022675. G6P_DH_C. IPR022674. G6P_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR23429. PTHR23429. 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...
Other
NextBio	603131.

Entry information

Entry name

G6PD_RAT

Accession

Primary (citable) accession number: P05370

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents