P52697 (6PGL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phosphogluconolactonase
Short name=6-P-gluconolactonase
Short name=Pgl
EC=3.1.1.31

Gene names

Name:	pgl
Synonyms:	ybhE
Ordered Locus Names:	b0767, JW0750

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. Ref.6
Catalytic activity	6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate. HAMAP MF_01605
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. HAMAP MF_01605
Sequence similarities	Belongs to the cycloisomerase 2 family.
Sequence caution	The sequence U27192 differs from that shown. Reason: Frameshift at position 110.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro
Molecular function	6-phosphogluconolactonase activity Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 331

331

6-phosphogluconolactonase HAMAP MF_01605

PRO_0000171132

Amino acid modifications

Modified residue

287

1

N6-acetyllysine Ref.7

Experimental info

Sequence conflict

37 – 52

16

QVQPM…RYLYV → RCSRWWSARTNVISML Ref.1

Sequence conflict

319 – 331

13

VGQGP…VVNAH → SGRDQCGWWLTHTKR Ref.1

Secondary structure

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331

Helix Strand Turn

Details...

Beta strand

2 – 9

8

Helix

10 – 12

3

Beta strand

14 – 20

7

Beta strand

26 – 33

8

Beta strand

41 – 43

3

Beta strand

47 – 54

8

Turn

55 – 58

4

Beta strand

59 – 65

7

Turn

67 – 69

3

Beta strand

72 – 79

8

Beta strand

85 – 89

5

Beta strand

93 – 100

8

Turn

101 – 104

4

Beta strand

105 – 112

8

Beta strand

115 – 123

9

Beta strand

138 – 145

8

Helix

146 – 148

3

Beta strand

150 – 156

7

Beta strand

162 – 171

10

Beta strand

178 – 183

6

Beta strand

187 – 194

8

Turn

195 – 198

4

Beta strand

199 – 206

8

Beta strand

213 – 219

7

Beta strand

231 – 236

6

Beta strand

240 – 247

8

Turn

248 – 251

4

Beta strand

252 – 258

7

Beta strand

265 – 272

8

Beta strand

274 – 276

3

Beta strand

280 – 282

3

Beta strand

286 – 292

7

Turn

294 – 296

3

Beta strand

298 – 305

8

Turn

306 – 309

4

Beta strand

310 – 318

9

Beta strand

320 – 322

3

Sequences

	Sequence		Length	Mass (Da)
	P52697 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: D731044CFCF31A8F	FASTA	331	36,308
	10 20 30 40 50 60 MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV 70 80 90 100 110 120 LAYRIAPDDG ALTFAAESAL PGSPTHISTD HQGQFVFVGS YNAGNVSVTR LEDGLPVGVV 130 140 150 160 170 180 DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH 190 200 210 220 230 240 MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG 250 260 270 280 290 300 RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NVDHSGKYLI AAGQKSHHIS 310 320 330 VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli." Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U., Gunsalus R.P., Shanmugam K.T. J. Bacteriol. 177:4851-4856(1995) [PubMed: 7665460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	Rudd K.E. Unpublished observations (MAR-1996) Cited for: IDENTIFICATION.
[6]	"Identification of the Escherichia coli K-12 ybhE gene as pgl, encoding 6-phosphogluconolactonase." Thomason L.C., Court D.L., Datta A.R., Khanna R., Rosner J.L. J. Bacteriol. 186:8248-8253(2004) [PubMed: 15576773] [Abstract] Cited for: FUNCTION. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[8]	"Structure of a putative 7-bladed propeller isomerase." Lima C.D., Kniewel R., Solorzano V., Wu J. Submitted (NOV-2003) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U27192 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC73854.1.
AP009048 Genomic DNA. Translation: BAA35431.1.

PIR

G64812.

RefSeq

NP_415288.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RI6	X-ray	2.00	A	2-331	[»]

ProteinModelPortal

P52697.

SMR

P52697. Positions 1-331.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52697. 5 interactions.

2D gel databases

2DBase-Ecoli

P52697.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004763; EBESCP00000004763; EBESCG00000003889.
EBESCT00000018358; EBESCP00000017649; EBESCG00000017412.

GeneID

946398.

GenomeReviews

Gene locus JW0750 in contig AP009048_GR.
Gene locus b0767 in contig U00096_GR.

KEGG

ecj:JW0750.
eco:b0767.

PATRIC

32116735. VBIEscCol129921_0793.

Organism-specific databases

EchoBASE

EB3020.

EcoGene

EG13231. pgl.

Phylogenomic databases

eggNOG

COG2706.

GeneTree

EBGT00050000009586.

HOGENOM

HBG741123.

OMA

CINELNS.

PhylomeDB

P52697.

ProtClustDB

PRK11028.

Enzyme and pathway databases

BioCyc

EcoCyc:6PGLUCONOLACT-MONOMER.
MetaCyc:6PGLUCONOLACT-MONOMER.

Gene expression databases

Genevestigator

P52697.

Family and domain databases

HAMAP

MF_01605. 6P-gluconolactonase.
[Tree]

InterPro

IPR022528. 6-phosphogluconolactonase_YbhE.
IPR019405. Lactonase_7-beta_prop.
IPR011045. N2O_reductase_N.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]

Gene3D

G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.

KO

K07404.

Pfam

PF10282. Lactonase. 1 hit.
[Graphical view]

SUPFAM

SSF50974. N2O_reductase_N. 1 hit.

ProtoNet

Search...

Entry information

Entry name

6PGL_ECOLI

Accession

Primary (citable) accession number: P52697
Secondary accession number(s): P75760

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program