[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00027085; PubMed=1643289 [NCBI, ExPASy, EBI, Israel, Japan] Scanlan D.J., Newman J., Sebaihia M., Mann N.H., Carr N.G.; "Cloning and sequence analysis of the glucose-6-phosphate dehydrogenase gene from the cyanobacterium Synechococcus PCC 7942."; Plant Mol. Biol. 19:877-880(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.; "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

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 .
SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U33285; AAA98847.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000100; ABB58364.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S23520; DEYCG6.

RefSeq

YP_401351.1; -.

3D structure databases

HSSP

P11413; 1QKI. [HSSP ENTRY / PDB]

ModBase

P29686.

Enzyme and pathway databases

BioCyc

SELO1140:SYNPCC7942_2334-MON; -.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004345;	Molecular function: glucose-6-phosphate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0006006;	Biological process: glucose metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001282; Glc-6-P_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR23429; G6PDH; 1.

Pfam

PF02781; G6PD_C; 1.
PF00479; G6PD_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000110; G6PD; 1.

PRINTS

PR00079; G6PDHDRGNASE.

ProDom

PD001129; G6PD; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00871; zwf; 1.

PROSITE

PS00069; G6P_DEHYDROGENASE; 1.

ProtoNet

P29686.

Genome annotation databases

GeneID

3774617; -.

GenomeReviews

CP000100_GR; Synpcc7942_2334.

KEGG

syf:Synpcc7942_2334; -.

Phylogenomic databases

HOGENOM

P29686; -.

Genome annotation databases

CMR

P29686; Synpcc7942_2334.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 511`	`511`	`Glucose-6-phosphate 1-dehydrogenase.`	`PRO_0000068134`
`ACT_SITE`	`260 260`		`Proton acceptor (By similarity).`
`BINDING`	`31 31`		`NADP (By similarity).`
`BINDING`	`63 63`		`NADP (By similarity).`
`BINDING`	`198 198`		`Substrate (By similarity).`
`BINDING`	`202 202`		`Substrate (By similarity).`
`BINDING`	`365 365`		`Substrate (By similarity).`
`CONFLICT`	`506 511`		`RRWRRL -> AVGVVSRIPATQLNSSGDV (in Ref. 1).`

Sequence information

Length: 511 AA [This is the length of the unprocessed precursor]

Molecular weight: 58095 Da [This is the MW of the unprocessed precursor]

CRC64: 9F16062520B51B10 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTPKLLENPL RIGLRQDKVP EPQILVIFGA TGDLTQRKLV PAIYEMHLER RLPPELTIVG 

        70         80         90        100        110        120 
VARRDWSDDY FREHLRQGVE QFGGGIQAEE VWNTFAQGLF FAPGNIDDPQ FYQTLRDRLA 

       130        140        150        160        170        180 
NLDELRGTRG NRTFYLSVAP RFFGEAAKQL GAAGMLADPA KTRLVVEKPF GRDLSSAQVL 

       190        200        210        220        230        240 
NAILQNVCRE SQIYRIDHYL GKETVQNLLV FRFANAIFEP LWNRQYIDHV QITVAETVGL 

       250        260        270        280        290        300 
EGRAGYYETA GALRDMVQNH LMQLFSLTAM EPPNSLGADG IRNEKVKVVQ ATRLADIDDL 

       310        320        330        340        350        360 
SLSAVRGQYK AGWMNGRSVP AYRDEEGADP QSFTPTYVAM KLLVDNWRWQ GVPFYLRTGK 

       370        380        390        400        410        420 
RMPKKVTEIA IQFKTVPHLM FQSATQKVNS PNVLVLRIQP NEGVSLRFEV KTPGSSQRTR 

       430        440        450        460        470        480 
SVDMDFRYDT AFGSPTQEAY SRLLVDCMLG DQTLFTRADE VEASWRVVTP LLESWDDPRQ 

       490        500        510 
AAGISFYEAG TWEPAEAEQL INRDGRRWRR L

P29686 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools