P31072 (6PGD_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phosphogluconate dehydrogenase, decarboxylating
EC=1.1.1.44

Gene names

Name:

GND

Organism

Trypanosoma brucei brucei

Taxonomic identifier

5702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Trypanozoon › Trypanosoma brucei

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH By similarity.
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 structure	Homodimer. Ref.2
Sequence similarities	Belongs to the 6-phosphogluconate dehydrogenase family.

Ontologies

Keywords
Biological process	Gluconate utilization Pentose shunt
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 479

479

6-phosphogluconate dehydrogenase, decarboxylating

PRO_0000090071

Regions

Nucleotide binding

9 – 14

6

NADP By similarity

Nucleotide binding

32 – 34

3

NADP By similarity

Nucleotide binding

77 – 79

3

NADP By similarity

Region

131 – 133

3

Substrate binding By similarity

Region

189 – 190

2

Substrate binding By similarity

Sites

Active site

186

1

Proton acceptor By similarity

Active site

193

1

Proton donor By similarity

Binding site

105

1

NADP By similarity

Binding site

105

1

Substrate By similarity

Binding site

194

1

Substrate By similarity

Binding site

263

1

Substrate; via amide nitrogen By similarity

Binding site

290

1

Substrate By similarity

Binding site

454

1

Substrate; shared with dimeric partner By similarity

Binding site

460

1

Substrate; shared with dimeric partner By similarity

Secondary structure

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479

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

12 – 23

12

Beta strand

28 – 31

4

Helix

35 – 44

10

Turn

45 – 47

3

Helix

51 – 53

3

Beta strand

54 – 56

3

Helix

60 – 66

7

Beta strand

72 – 75

4

Helix

81 – 93

13

Beta strand

99 – 102

4

Helix

108 – 119

12

Turn

120 – 122

3

Beta strand

124 – 132

9

Helix

133 – 139

7

Beta strand

142 – 147

6

Helix

149 – 162

14

Helix

181 – 209

29

Helix

214 – 226

13

Helix

233 – 243

11

Beta 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

Beta strand

370 – 373

4

Helix

380 – 389

10

Helix

398 – 400

3

Helix

401 – 421

21

Helix

427 – 439

13

Helix

446 – 458

13

Beta strand

462 – 471

10

Sequences

	Sequence		Length	Mass (Da)
	P31072 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 64FED260915ABC2F	FASTA	479	52,154
	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

References

[1]

"A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei." Barrett M.P., le Page R.W.F. Mol. Biochem. Parasitol. 57:89-100(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 427.

[2]

"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." Phillips C., Dohnalek J., Gover S., Barrett M.P., Adams M.J. J. Mol. Biol. 282:667-681(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X65623 Genomic DNA. Translation: CAA46577.1.

PIR

A48565.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PGJ	X-ray	2.82	A/B	2-479	[»]

ProteinModelPortal

P31072.

SMR

P31072. Positions 2-479.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

EuPathDB

TriTrypDB:Tb09.211.3180.

Enzyme and pathway databases

UniPathway

UPA00115; UER00410.

Family and domain databases

Gene3D

1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.

InterPro

IPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_decarbox.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Pfam

PF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]

PIRSF

PIRSF000109. 6PGD. 1 hit.

SUPFAM

SSF48179. 6DGDH_C_like. 1 hit.

TIGRFAMs

TIGR00873. gnd. 1 hit.

PROSITE

PS00461. 6PGD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P31072.

Entry information

Entry name

6PGD_TRYBB

Accession

Primary (citable) accession number: P31072

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 29, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)