Reviewed, UniProtKB/Swiss-Prot P37754 (6PGD9_ECOLX)

Names and origin

Protein names

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

Gene names

Name:

gnd

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH.
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
Sequence similarities	Belongs to the 6-phosphogluconate dehydrogenase family.

Ontologies

Keywords
Biological process	Gluconate utilization Pentose shunt
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 468	468	6-phosphogluconate dehydrogenase, decarboxylating		PRO_0000090038

Sequences

	Sequence		Length	Mass (Da)
	P37754-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: C13D94CFD78BFF3A	FASTA	468	51,625
	10 20 30 40 50 60 MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENPGKK LVPYYTVQEF 70 80 90 100 110 120 VESLETPRRI LLMVKAGSGT DSAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF 130 140 150 160 170 180 NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILKQIA AVAEDGEPCV TYIGADGAGH 190 200 210 220 230 240 YVKMVHNGIE YGDMQLIAEA YALLKGGLTL SNEELAQTFT EWNEGELSSY LYDITKDIFT 250 260 270 280 290 300 KKDEEGKYLV DVILDEAANK GTGKWTSQSS LDLGEPLSLI TESVFPRYIS SLKDQRVAAS 310 320 330 340 350 360 KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASDEYNWE LNYAEIAKIF 370 380 390 400 410 420 RAGCIIRAQF LQKITDAYAQ NAGIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIRVPT 430 440 450 460 FSAAIAYYDS YRSAVLPANL IQAQRDYFGA HTYKRTDKEG VFHTEWLE

References

[1]

"Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli O9:K30 and participation of rfb genes in the synthesis of the group I K30 capsular polysaccharide." Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., Whitfield C. J. Bacteriol. 176:3126-3139(1994) [PubMed: 7515042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O9:K30:H12 / E69.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L27646 Genomic DNA. Translation: AAA21136.1.
PIR	I41250.
3D structure databases
HSSP	HSSP built from PDB template 2PGD based on UniProtKB P00349.
ModBase	Search...
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]
Gene3D	G3DSA:1.20.5.320. Fibritin/6PGD_C-extension. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
Pfam	PF00393. 6PGD. 1 hit. PF03446. NAD_binding_2. 1 hit. [Graphical view]
PRINTS	PR00076. 6PGDHDRGNASE.
TIGRFAMs	TIGR00873. gnd. 1 hit.
PROSITE	PS00461. 6PGD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

6PGD9_ECOLX

Accession

Primary (citable) accession number: P37754

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 25, 2008
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)