Skip Header

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

Fructose-like phosphotransferase enzyme IIB component 3

Gene

frwD

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

Functioni

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.By similarity

Catalytic activityi

[Protein]-N(pi)-phospho-L-histidine + D-fructose(Side 1) = [protein]-L-histidine + D-fructose 1-phosphate(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Phosphocysteine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11912-MONOMER.
ECOL316407:JW3925-MONOMER.

Protein family/group databases

TCDBi4.A.2.1.10. the pts fructose-mannitol (fru) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-like phosphotransferase enzyme IIB component 3 (EC:2.7.1.202)
Alternative name(s):
PTS system fructose-like EIIB component 3
Gene namesi
Name:frwD
Synonyms:yijN
Ordered Locus Names:b3953, JW3925
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11912. frwD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 113113Fructose-like phosphotransferase enzyme IIB component 3PRO_0000186505Add
BLAST

Proteomic databases

PaxDbiP32676.
PRIDEiP32676.

Interactioni

Protein-protein interaction databases

BioGridi4263010. 6 interactions.
IntActiP32676. 2 interactions.
STRINGi511145.b3953.

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Turni13 – 175Combined sources
Helixi18 – 3013Combined sources
Beta strandi34 – 418Combined sources
Beta strandi44 – 474Combined sources
Helixi51 – 566Combined sources
Beta strandi58 – 669Combined sources
Helixi71 – 744Combined sources
Beta strandi79 – 824Combined sources
Helixi84 – 896Combined sources
Helixi92 – 10312Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi108 – 1114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TN5X-ray2.29A/B1-113[»]
ProteinModelPortaliP32676.
SMRiP32676. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 100100PTS EIIB type-2PROSITE-ProRule annotationAdd
BLAST

Domaini

The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.

Sequence similaritiesi

Contains 1 PTS EIIB type-2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108XCZ. Bacteria.
COG1445. LUCA.
HOGENOMiHOG000231313.
KOiK11202.
OMAiCQQEKWN.
OrthoDBiEOG6XDGX2.
PhylomeDBiP32676.

Family and domain databases

InterProiIPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003353. PTS_IIB_fruc.
[Graphical view]
PfamiPF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
TIGRFAMsiTIGR00829. FRU. 1 hit.
PROSITEiPS51099. PTS_EIIB_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYLVAVTAC VSGVAHTYMA AERLEKLCLL EKWGVSIETQ GALGTENRLA
60 70 80 90 100
DEDIRRADVA LLITDIELAG AERFEHCRYV QCSIYAFLRE PQRVMSAVRK
110
VLSAPQQTHL ILE
Length:113
Mass (Da):12,637
Last modified:October 1, 1993 - v1
Checksum:i36252AB21DDB09EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43059.1.
U00096 Genomic DNA. Translation: AAC76935.1.
AP009048 Genomic DNA. Translation: BAE77358.1.
PIRiD65202.
RefSeqiNP_418388.1. NC_000913.3.
WP_000323846.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76935; AAC76935; b3953.
BAE77358; BAE77358; BAE77358.
GeneIDi948452.
KEGGiecj:JW3925.
eco:b3953.
PATRICi32123427. VBIEscCol129921_4074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43059.1.
U00096 Genomic DNA. Translation: AAC76935.1.
AP009048 Genomic DNA. Translation: BAE77358.1.
PIRiD65202.
RefSeqiNP_418388.1. NC_000913.3.
WP_000323846.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TN5X-ray2.29A/B1-113[»]
ProteinModelPortaliP32676.
SMRiP32676. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263010. 6 interactions.
IntActiP32676. 2 interactions.
STRINGi511145.b3953.

Protein family/group databases

TCDBi4.A.2.1.10. the pts fructose-mannitol (fru) family.

Proteomic databases

PaxDbiP32676.
PRIDEiP32676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76935; AAC76935; b3953.
BAE77358; BAE77358; BAE77358.
GeneIDi948452.
KEGGiecj:JW3925.
eco:b3953.
PATRICi32123427. VBIEscCol129921_4074.

Organism-specific databases

EchoBASEiEB1856.
EcoGeneiEG11912. frwD.

Phylogenomic databases

eggNOGiENOG4108XCZ. Bacteria.
COG1445. LUCA.
HOGENOMiHOG000231313.
KOiK11202.
OMAiCQQEKWN.
OrthoDBiEOG6XDGX2.
PhylomeDBiP32676.

Enzyme and pathway databases

BioCyciEcoCyc:EG11912-MONOMER.
ECOL316407:JW3925-MONOMER.

Miscellaneous databases

PROiP32676.

Family and domain databases

InterProiIPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003353. PTS_IIB_fruc.
[Graphical view]
PfamiPF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
TIGRFAMsiTIGR00829. FRU. 1 hit.
PROSITEiPS51099. PTS_EIIB_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Novel phosphotransferase system genes revealed by bacterial genome analysis -- a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system."
    Reizer J., Reizer A., Saier M.H. Jr.
    Microbiology 141:961-971(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.

Entry informationi

Entry nameiPTFB3_ECOLI
AccessioniPrimary (citable) accession number: P32676
Secondary accession number(s): Q2M8P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 11, 2016
This is version 124 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.