NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
Wesolowski-Louvel M., Tanguy-Rougeau C., Fukuhara H.;
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).

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

X70373; CAA49834.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382124; CAH01040.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S31337; S31337.

RefSeq

XP_453944.1; -.

3D structure databases

HSSP

P11413; 1QKI. [HSSP ENTRY / PDB]

ModBase

P48828.

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

P48828.

Genome annotation databases

GeneID

2893289; -.

KEGG

kla:KLLA0D19855g; -.

Phylogenomic databases

HOGENOM

P48828; -.

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`	`1 497`	`497`	`Glucose-6-phosphate 1-dehydrogenase.`	`PRO_0000068104`
`ACT_SITE`	`245 245`		`Proton acceptor (By similarity).`
`BINDING`	`17 17`		`NADP (By similarity).`
`BINDING`	`49 49`		`NADP (By similarity).`
`BINDING`	`183 183`		`Substrate (By similarity).`
`BINDING`	`187 187`		`Substrate (By similarity).`

Sequence information

Length: 497 AA [This is the length of the unprocessed precursor]

Molecular weight: 56574 Da [This is the MW of the unprocessed precursor]

CRC64: C6EC57AD6B6E9F1F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATQFDENTV ITIFGASGDL SKKKTFPALF GLYREGYLNP TTKIIGYARS KLSNEDLREK 

        70         80         90        100        110        120 
VKPFLKKPNG AKDDAKVNEF LSMVSYHAGP YDSDEGYLEL KKIIEEFEAE KKVDEPHRLF 

       130        140        150        160        170        180 
YLALPPSIFI DVCSKLKENL YTESGIQRVI VEKPFGHDLQ SATELQEKLA PLFSEDELFR 

       190        200        210        220        230        240 
IDHYLGKEMV KNLLLMRFGN TFLNAAWNKE NIQSVQVVFK EPFGTEGRGG YFDSIGIIRD 

       250        260        270        280        290        300 
VMQNHLLQVL TLLTMERPVS FDPESVRDEK VKVLKAFSPI DHDDILIGQY GRSVDGSKPS 

       310        320        330        340        350        360 
YLDDETVKED SKCVTFAAIG FKIANERWDG VPIVMRAGKA LNEGKVEIRI QFRRVASGMF 

       370        380        390        400        410        420 
TDIPNNELVI RIQPNEAIYL KCNAKTPGLA NENQTTELDL TYSERYKNYW IPEAYESLIR 

       430        440        450        460        470        480 
DALLGDHSNF VRDDELDVSW KLFTPLLNYL EGPDGPQPKI YPYGCRSPDG LVEFLADHGY 

       490 
TFSKPGSYQW PVTTPKM

P48828 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