Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P52697

- 6PGL_ECOLI

UniProt

P52697 - 6PGL_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

6-phosphogluconolactonase

Gene

pgl

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.1 Publication

Catalytic activityi

6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate.

Pathwayi

GO - Molecular functioni

  1. 6-phosphogluconolactonase activity Source: EcoliWiki

GO - Biological processi

  1. pentose-phosphate shunt Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Enzyme and pathway databases

BioCyciEcoCyc:6PGLUCONOLACT-MONOMER.
ECOL316407:JW0750-MONOMER.
MetaCyc:6PGLUCONOLACT-MONOMER.
UniPathwayiUPA00115; UER00409.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphogluconolactonase (EC:3.1.1.31)
Short name:
6-P-gluconolactonase
Short name:
Pgl
Gene namesi
Name:pgl
Synonyms:ybhE
Ordered Locus Names:b0767, JW0750
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG13231. pgl.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3313316-phosphogluconolactonasePRO_0000171132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei287 – 2871N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP52697.
PRIDEiP52697.

Expressioni

Gene expression databases

GenevestigatoriP52697.

Interactioni

Protein-protein interaction databases

IntActiP52697. 5 interactions.
STRINGi511145.b0767.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi10 – 123Combined sources
Beta strandi14 – 207Combined sources
Beta strandi26 – 338Combined sources
Beta strandi41 – 433Combined sources
Beta strandi47 – 548Combined sources
Turni55 – 584Combined sources
Beta strandi59 – 657Combined sources
Turni67 – 693Combined sources
Beta strandi72 – 798Combined sources
Beta strandi85 – 895Combined sources
Beta strandi93 – 1008Combined sources
Turni101 – 1044Combined sources
Beta strandi105 – 1128Combined sources
Beta strandi115 – 1239Combined sources
Beta strandi138 – 1458Combined sources
Helixi146 – 1483Combined sources
Beta strandi150 – 1567Combined sources
Beta strandi162 – 17110Combined sources
Beta strandi178 – 1836Combined sources
Beta strandi187 – 1948Combined sources
Turni195 – 1984Combined sources
Beta strandi199 – 2068Combined sources
Beta strandi213 – 2197Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi240 – 2478Combined sources
Turni248 – 2514Combined sources
Beta strandi252 – 2587Combined sources
Beta strandi265 – 2728Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi286 – 2927Combined sources
Turni294 – 2963Combined sources
Beta strandi298 – 3058Combined sources
Turni306 – 3094Combined sources
Beta strandi310 – 3189Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi325 – 3317Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RI6X-ray2.00A2-331[»]
ProteinModelPortaliP52697.
SMRiP52697. Positions 1-331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52697.

Family & Domainsi

Sequence similaritiesi

Belongs to the cycloisomerase 2 family.Curated

Phylogenomic databases

eggNOGiCOG2706.
HOGENOMiHOG000257418.
InParanoidiP52697.
KOiK07404.
OMAiDKRFLYV.
OrthoDBiEOG615VK7.
PhylomeDBiP52697.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_01605. 6P_gluconolactonase.
InterProiIPR022528. 6-phosphogluconolactonase_YbhE.
IPR019405. Lactonase_7-beta_prop.
IPR011045. N2O_reductase_N.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF10282. Lactonase. 1 hit.
[Graphical view]
SUPFAMiSSF50974. SSF50974. 1 hit.

Sequencei

Sequence statusi: Complete.

P52697 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL
60 70 80 90 100
YVGVRPEFRV LAYRIAPDDG ALTFAAESAL PGSPTHISTD HQGQFVFVGS
110 120 130 140 150
YNAGNVSVTR LEDGLPVGVV DVVEGLDGCH SANISPDNRT LWVPALKQDR
160 170 180 190 200
ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH MVFHPNEQYA YCVNELNSSV
210 220 230 240 250
DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG RHLYACDRTA
260 270 280 290 300
SLITVFSVSE DGSVLSKEGF QPTETQPRGF NVDHSGKYLI AAGQKSHHIS
310 320 330
VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H
Length:331
Mass (Da):36,308
Last modified:November 1, 1997 - v2
Checksum:iD731044CFCF31A8F
GO

Sequence cautioni

The sequence U27192 differs from that shown. Reason: Frameshift at position 110.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 5216QVQPM…RYLYV → RCSRWWSARTNVISML(PubMed:7665460)CuratedAdd
BLAST
Sequence conflicti319 – 33113VGQGP…VVNAH → SGRDQCGWWLTHTKR(PubMed:7665460)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U27192 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC73854.1.
AP009048 Genomic DNA. Translation: BAA35431.1.
PIRiG64812.
RefSeqiNP_415288.1. NC_000913.3.
YP_489040.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73854; AAC73854; b0767.
BAA35431; BAA35431; BAA35431.
GeneIDi12932157.
946398.
KEGGiecj:Y75_p0740.
eco:b0767.
PATRICi32116735. VBIEscCol129921_0793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U27192 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC73854.1 .
AP009048 Genomic DNA. Translation: BAA35431.1 .
PIRi G64812.
RefSeqi NP_415288.1. NC_000913.3.
YP_489040.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RI6 X-ray 2.00 A 2-331 [» ]
ProteinModelPortali P52697.
SMRi P52697. Positions 1-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P52697. 5 interactions.
STRINGi 511145.b0767.

Proteomic databases

PaxDbi P52697.
PRIDEi P52697.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73854 ; AAC73854 ; b0767 .
BAA35431 ; BAA35431 ; BAA35431 .
GeneIDi 12932157.
946398.
KEGGi ecj:Y75_p0740.
eco:b0767.
PATRICi 32116735. VBIEscCol129921_0793.

Organism-specific databases

EchoBASEi EB3020.
EcoGenei EG13231. pgl.

Phylogenomic databases

eggNOGi COG2706.
HOGENOMi HOG000257418.
InParanoidi P52697.
KOi K07404.
OMAi DKRFLYV.
OrthoDBi EOG615VK7.
PhylomeDBi P52697.

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00409 .
BioCyci EcoCyc:6PGLUCONOLACT-MONOMER.
ECOL316407:JW0750-MONOMER.
MetaCyc:6PGLUCONOLACT-MONOMER.

Miscellaneous databases

EvolutionaryTracei P52697.
PROi P52697.

Gene expression databases

Genevestigatori P52697.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
HAMAPi MF_01605. 6P_gluconolactonase.
InterProi IPR022528. 6-phosphogluconolactonase_YbhE.
IPR019405. Lactonase_7-beta_prop.
IPR011045. N2O_reductase_N.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view ]
Pfami PF10282. Lactonase. 1 hit.
[Graphical view ]
SUPFAMi SSF50974. SSF50974. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, IDENTIFICATION BY 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).

Entry informationi

Entry namei6PGL_ECOLI
AccessioniPrimary (citable) accession number: P52697
Secondary accession number(s): P75760
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3