NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(87)90100-5; PubMed=2822568 [NCBI, ExPASy, EBI, Israel, Japan]
Kaslow D.C., Migeon B.R., Persico M.G., Zollo M., Vandeberg J.L., Samollow P.B.;
"Molecular studies of marsupial X chromosomes reveal limited sequence homology of mammalian X-linked genes.";
Genomics 1:19-28(1987).

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

M19637; AAA30971.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19636; AAA30971.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19642; AAA30972.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19638; AAA30973.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19639; AAA30974.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19641; AAA30975.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19640; AAA30975.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P11413; 1QKI. [HSSP ENTRY / PDB]

SMR

P15588; 53-100, 132-191.

ModBase

P15588.

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; 2.
Pfam graphical view of domain structure.

PROSITE

PS00069; G6P_DEHYDROGENASE; PARTIAL.

BLOCKS

P15588.

Phylogenomic databases

HOVERGEN

P15588; -.

Other

ProtoNet

P15588.

UniRef

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

Keywords

Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 191`	`191`	`Glucose-6-phosphate 1-dehydrogenase.`	`PRO_0000068082`
`ACT_SITE`	`106 106`		`Proton acceptor (By similarity).`
`BINDING`	`40 40`		`NADP (By similarity).`
`MOD_RES`	`179 179`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`183 183`		`Phosphotyrosine (By similarity).`
`NON_CONS`	`52 53`
`NON_CONS`	`100 101`
`NON_CONS`	`131 132`

Sequence information

Length: 191 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 21941 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: E838F22AA83F4AFD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEQVALSRT QVCGILREEL YQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIEPASFQRL 

        70         80         90        100        110        120 
NTHMNSLHHG AQANRLFYLA LPPIVYEAVT KNIKETCMSQ DVMQNHLLQM LCLVAMEKPA 

       130        140        150        160        170        180 
STNSDDVRDE KDELQEAWRI FTPLLHHIER EKTQPIPYVY GSRGPPEADE LMKRVGFQYE 

       190 
GTYKWVNPHK L

P15588 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