NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=427;
DOI=10.1016/0166-6851(93)90247-U; PubMed=8426618 [NCBI, ExPASy, EBI, Israel, Japan]
Barrett M.P., le Page R.W.F.;
"A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei.";
Mol. Biochem. Parasitol. 57:89-100(1993).

[2]

X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1006/jmbi.1998.2059; PubMed=9737929 [NCBI, ExPASy, EBI, Israel, Japan]
Phillips C., Dohnalek J., Gover S., Barrett M.P., Adams M.J.;
"A 2.8-A resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues.";
J. Mol. Biol. 282:667-681(1998).

Comments

CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP⁺ = D-ribulose 5-phosphate + CO₂ + NADPH.
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3 .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the 6-phosphogluconate 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

X65623; CAA46577.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A48565; A48565.

3D structure databases

PDB

1PGJ; X-ray; 2.82 A; A/B=2-479.

[ExPASy / RCSB / EBI]

PDBsum

1PGJ; -.

ModBase

P31072.

Ontologies

GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004616;	Molecular function: phosphogluconate dehydrogenase (decarboxylating) activity (inferred from electronic annotation from InterPro).
GO:0019521;	Biological process: D-gluconate metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006098;	Biological process: pentose-phosphate shunt (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006183; 6-phosphogluconate_DHase.
IPR006114; 6PGDH_C.
IPR006113; 6PGDH_decarbox.
IPR006115; 6PGDH_NAD-bd.
IPR006184; 6PGdom_BS.
IPR013328; DHase_multihelical.
IPR012284; Fibritin/6PGD_C-extension.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF00393; 6PGD; 1.
PF03446; NAD_binding_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00076; 6PGDHDRGNASE.

TIGR00873; gnd; 1.

PS00461; 6PGD; 1.

Other

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

Keywords

3D-structure; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 479`	`479`	`6-phosphogluconate dehydrogenase, decarboxylating.`	`PRO_0000090071`
`STRAND`	`3 8`	`6`
`HELIX`	`12 23`	`12`
`STRAND`	`28 31`	`4`
`HELIX`	`35 44`	`10`
`TURN`	`45 47`	`3`
`HELIX`	`51 53`	`3`
`STRAND`	`54 56`	`3`
`HELIX`	`60 66`	`7`
`STRAND`	`72 75`	`4`
`HELIX`	`81 93`	`13`
`STRAND`	`99 102`	`4`
`HELIX`	`108 119`	`12`
`TURN`	`120 122`	`3`
`STRAND`	`124 132`	`9`
`HELIX`	`133 139`	`7`
`STRAND`	`142 147`	`6`
`HELIX`	`149 162`	`14`
`HELIX`	`181 209`	`29`
`HELIX`	`214 226`	`13`
`HELIX`	`233 243`	`11`
`STRAND`	`249 251`	`3`
`HELIX`	`252 255`	`4`
`HELIX`	`265 276`	`12`
`HELIX`	`281 294`	`14`
`HELIX`	`296 305`	`10`
`TURN`	`307 310`	`4`
`HELIX`	`325 356`	`32`
`HELIX`	`362 367`	`6`
`STRAND`	`370 373`	`4`
`HELIX`	`380 389`	`10`
`HELIX`	`398 400`	`3`
`HELIX`	`401 421`	`21`
`HELIX`	`427 439`	`13`
`HELIX`	`446 458`	`13`
`STRAND`	`462 471`	`10`

Sequence information

Length: 479 AA [This is the length of the unprocessed precursor]

Molecular weight: 52154 Da [This is the MW of the unprocessed precursor]

CRC64: 64FED260915ABC2F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSMDVGVVGL GVMGANLALN IAEKGFKVAV FNRTYSKSEE FMKANASAPF AGNLKAFETM 

        70         80         90        100        110        120 
EAFAASLKKP RKALILVQAG AATDSTTEQL KKVFEKGDIL VDTGNAHFKD QGRRAQQLEA 

       130        140        150        160        170        180 
AGLRFLGMGI SGGEEGARKG PAFFPGGTLS VWEEIRPIVE AAAAKADDGR PCVTMNGSGG 

       190        200        210        220        230        240 
AGSCVKMYHN SGEYAILQIW GEVFDILRAM GLNNDEVAAV LEDWKSKNFL KSYMLDISIA 

       250        260        270        280        290        300 
AARAKDKDGS YLTEHVMDRI GSKGTGLWSA QEALEIGVPA PSLNMAVVSR QFTMYKTERQ 

       310        320        330        340        350        360 
ANASNAPGIT QSPGYTLKNK SPSGPEIKQL YDSVCIAIIS CYAQMFQCLR EMDKVHNFGL 

       370        380        390        400        410        420 
NLPATIATFR AGCILQGYLL KPMTEAFEKN PNISNLMCAF QTEIRAGLQN YRDMVALITS 

       430        440        450        460        470 
KLEVSIPVLS ASLNYVTAMF TPTLKYGQLV SLQRDVFGRH GYERVDKDGR ESFQWPELQ

P31072 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