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Entry version 125 (07 Oct 2020)
Sequence version 1 (19 Jul 2005)
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Protein

Fructose-1,6-bisphosphatase 1 class 2

Gene

glpX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Is likely to be involved in gluconeogenesis during growth on glycerol. Also displays a low activity toward glucose 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate, fructose 2,6-bisphosphate, or fructose 1-phosphate.2 Publications

Miscellaneous

E.coli K12 also possesses a FBPase class 1 (Fbp), which is the primary FBPase in E.coli and probably represents the main gluconeogenic FBPase.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+2 PublicationsNote: Manganese. Mg2+, Co2+, Ni2+, Ca2+, Cu2+ and Zn2+ cannot support activity.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Competitively inhibited by low concentrations of phosphate (IC50 3.0 mM) and is also sensitive to Li+ (IC50 70 mM). Slightly activated by KCl.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

The catalytic efficiency of GlpX is 3-fold higher than that of YggF, the other FBPase class 2 in E.coli.
  1. KM=35 µM for fructose 1,6-bisphosphate (at pH 7.7 and room temperature)2 Publications
  2. KM=70 µM for fructose 1,6-bisphosphate (at pH 9.0 and 37 degrees Celsius)2 Publications
  3. KM=0.6 mM for Mn2+ (at pH 9.0 and 37 degrees Celsius)2 Publications
  1. Vmax=3.3 µmol/min/mg enzyme (at pH 7.7 and room temperature)2 Publications
  2. Vmax=8.8 µmol/min/mg enzyme (at pH 9.0 and 37 degrees Celsius)2 Publications

pH dependencei

Optimum pH is 7.5-8.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi33Manganese 11 Publication1
Metal bindingi57Manganese 11 Publication1
Metal bindingi85Manganese 21 Publication1
Metal bindingi88Manganese 21 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei119Substrate1 Publication1
Binding sitei210Substrate; via amide nitrogen1 Publication1
Metal bindingi213Manganese 21 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processCarbohydrate metabolism
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11517-MONOMER
MetaCyc:EG11517-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.3.11, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A9C9

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00138

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase 1 class 2 (EC:3.1.3.11)
Short name:
FBPase 1 class 2
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1 class 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:glpX
Ordered Locus Names:b3925, JW3896
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene grow normally on gluconeogenic substrates (succinate or glycerol).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi29K → A: 2.4-fold increase in FBPase activity, and no effect on substrate affinity. 1 Publication1
Mutagenesisi57E → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi59E → A: 5.5-fold decrease in FBPase activity, and 1.4-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi61D → A: Great decrease in FBPase activity. 1 Publication1
Mutagenesisi85D → A: Great decrease in FBPase activity. 1 Publication1
Mutagenesisi88E → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi90T → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi119Y → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi164K → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi166R → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi186D → A: 5-fold decrease in FBPase activity, and 3-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi188D → A: Great decrease in FBPase activity. 1 Publication1
Mutagenesisi213E → A: Great decrease in FBPase activity. 1 Publication1
Mutagenesisi235R → A: Nearly no effect on FBPase activity, and 3-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi239K → A: 1.3-fold increase in FBPase activity, and 1.4-fold decrease in substrate affinity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002011001 – 336Fructose-1,6-bisphosphatase 1 class 2Add BLAST336

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9C9

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A9C9

PRoteomics IDEntifications database

More...
PRIDEi
P0A9C9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By glycerol and sn-glycerol-3-phosphate.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260756, 16 interactors
852721, 1 interactor

Protein interaction database and analysis system

More...
IntActi
P0A9C9, 6 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3925

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A9C9

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A9C9

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni88 – 90Substrate binding1 Publication3
Regioni164 – 166Substrate binding1 Publication3
Regioni186 – 188Substrate binding1 Publication3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the FBPase class 2 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1494, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_054938_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9C9

KEGG Orthology (KO)

More...
KOi
K02446

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9C9

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01516, FBPase_glpX, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004464, FBPase_class-2/SBPase

The PANTHER Classification System

More...
PANTHERi
PTHR30447, PTHR30447, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03320, FBPase_glpX, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF004532, GlpX, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00330, glpX, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0A9C9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRRELAIEFS RVTESAALAG YKWLGRGDKN TADGAAVNAM RIMLNQVNID
60 70 80 90 100
GTIVIGEGEI DEAPMLYIGE KVGTGRGDAV DIAVDPIEGT RMTAMGQANA
110 120 130 140 150
LAVLAVGDKG CFLNAPDMYM EKLIVGPGAK GTIDLNLPLA DNLRNVAAAL
160 170 180 190 200
GKPLSELTVT ILAKPRHDAV IAEMQQLGVR VFAIPDGDVA ASILTCMPDS
210 220 230 240 250
EVDVLYGIGG APEGVVSAAV IRALDGDMNG RLLARHDVKG DNEENRRIGE
260 270 280 290 300
QELARCKAMG IEAGKVLRLG DMARSDNVIF SATGITKGDL LEGISRKGNI
310 320 330
ATTETLLIRG KSRTIRRIQS IHYLDRKDPE MQVHIL
Length:336
Mass (Da):35,852
Last modified:July 19, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDEC2A477E5C4062E
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence M19644 differs from that shown. The C-terminal part of glpX was incorrectly assigned as being part of mvrA.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z11767 Genomic DNA Translation: CAA77814.1
L19201 Genomic DNA Translation: AAB03057.1
U00096 Genomic DNA Translation: AAC76907.1
AP009048 Genomic DNA Translation: BAE77385.1
M19644 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
A45248

NCBI Reference Sequences

More...
RefSeqi
NP_418360.1, NC_000913.3
WP_001250644.1, NZ_STEB01000017.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76907; AAC76907; b3925
BAE77385; BAE77385; BAE77385

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
49586796
948424

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3896
eco:b3925

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2780

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11767 Genomic DNA Translation: CAA77814.1
L19201 Genomic DNA Translation: AAB03057.1
U00096 Genomic DNA Translation: AAC76907.1
AP009048 Genomic DNA Translation: BAE77385.1
M19644 Genomic DNA No translation available.
PIRiA45248
RefSeqiNP_418360.1, NC_000913.3
WP_001250644.1, NZ_STEB01000017.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NI9X-ray2.00A1-336[»]
2R8TX-ray2.30A1-336[»]
3BIGX-ray1.85A1-336[»]
3BIHX-ray2.10A1-336[»]
3D1RX-ray1.85A1-336[»]
SMRiP0A9C9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260756, 16 interactors
852721, 1 interactor
IntActiP0A9C9, 6 interactors
STRINGi511145.b3925

Proteomic databases

jPOSTiP0A9C9
PaxDbiP0A9C9
PRIDEiP0A9C9

Genome annotation databases

EnsemblBacteriaiAAC76907; AAC76907; b3925
BAE77385; BAE77385; BAE77385
GeneIDi49586796
948424
KEGGiecj:JW3896
eco:b3925
PATRICifig|1411691.4.peg.2780

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1479

Phylogenomic databases

eggNOGiCOG1494, Bacteria
HOGENOMiCLU_054938_0_0_6
InParanoidiP0A9C9
KOiK02446
PhylomeDBiP0A9C9

Enzyme and pathway databases

UniPathwayiUPA00138
BioCyciEcoCyc:EG11517-MONOMER
MetaCyc:EG11517-MONOMER
BRENDAi3.1.3.11, 2026
SABIO-RKiP0A9C9

Miscellaneous databases

EvolutionaryTraceiP0A9C9

Protein Ontology

More...
PROi
PR:P0A9C9

Family and domain databases

CDDicd01516, FBPase_glpX, 1 hit
InterProiView protein in InterPro
IPR004464, FBPase_class-2/SBPase
PANTHERiPTHR30447, PTHR30447, 1 hit
PfamiView protein in Pfam
PF03320, FBPase_glpX, 1 hit
PIRSFiPIRSF004532, GlpX, 1 hit
TIGRFAMsiTIGR00330, glpX, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLPX_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A9C9
Secondary accession number(s): P11007
, P28860, P28900, Q2M8M1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 7, 2020
This is version 125 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
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