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Entry version 163 (12 Aug 2020)
Sequence version 2 (15 Jul 1998)
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Protein

Fructose-6-phosphate aldolase 1

Gene

fsaA

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 reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D---threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, sedoheptulose 1,7-bisphosphate, xylulose 5-phosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate; cannot use dihydroxyacetone phosphate as donor compound nor D-glyceraldehyde as acceptor. Does not display transaldolase activity.4 Publications

Miscellaneous

Is not inhibited by EDTA which points to a metal-independent mode of action.1 Publication

<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 <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

Inhibited by glycerol, inorganic phosphate and arabinose 5-phosphate.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

kcat is 1.31 sec(-1), 0.82 sec(-1) and 0.63 sec(-1) using glyceraldehyde 3-phosphate as acceptor substrate, and dihydroxyacetone, hydroxyacetone or 1-hydroxy-butan-2-one as donor substrate, respectively (at 25 degrees Celsius and pH 8.5).1 Publication
  1. KM=9 mM for D-fructose 6-phosphate (at 30 degrees Celsius and pH 8.5)1 Publication
  2. KM=35 mM for dihydroxyacetone (at 30 degrees Celsius and pH 8.5)1 Publication
  3. KM=0.8 mM for glyceraldehyde 3-phosphate (at 30 degrees Celsius and pH 8.5)1 Publication
  4. KM=40 mM for dihydroxyacetone (at 25 degrees Celsius and pH 8.5)1 Publication
  5. KM=11 mM for hydroxyacetone (at 25 degrees Celsius and pH 8.5)1 Publication
  6. KM=32 mM for 1-hydroxy-butan-2-one (at 25 degrees Celsius and pH 8.5)1 Publication
  7. KM=32 mM for dihydroxyacetone1 Publication
  8. KM=17.4 mM for hydroxyacetone1 Publication
  9. KM=0.197 mM for glycolaldehyde (as donor substrate in the self-aldol addition of glycolaldehyde)1 Publication
  10. KM=62.8 mM for glycolaldehyde (as acceptor substrate in the self-aldol addition of glycolaldehyde)1 Publication
  11. KM=0.286 mM for D-threose1 Publication
  12. KM=0.561 mM for D-arabinose-5-P1 Publication
  1. Vmax=45 µmol/min/mg enzyme for the aldolization reaction leading to D-fructose 6-phosphate (at 30 degrees Celsius and pH 8.5)1 Publication
  2. Vmax=7 µmol/min/mg enzyme for D-fructose 6-phosphate cleavage (at 30 degrees Celsius and pH 8.5)1 Publication
  3. Vmax=1.46 µmol/min/mg enzyme for the aldol reaction with DHA and D,L-glyceraldehyde 3-phosphate as substrates1 Publication
  4. Vmax=33.7 µmol/min/mg enzyme for the aldol reaction with HA and D,L-glyceraldehyde 3-phosphate as substrates1 Publication
  5. Vmax=0.22 µmol/min/mg enzyme for the self-aldol addition of glycolaldehyde1 Publication
  6. Vmax=0.34 µmol/min/mg enzyme for D-fructose 6-phosphate cleavage1 Publication
  7. Vmax=0.160 µmol/min/mg enzyme for D-arabinose-5-P cleavage1 Publication

pH dependencei

Optimum pH is about 8.5. Active from pH 6 to 12.1 Publication

Temperature dependencei

Displays a broad temperature optimum and is active in the range from 20 to 75 degrees Celsius. Although no significant loss of activity is detected after 600 hours of incubation at 45 degrees Celsius (at pH 8.0), the respective half-lives of the enzyme are 200 hours at 55 degrees Celsius, 30 hours at 65 degrees Celsius, and 16 hours at 75 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei85Schiff-base intermediate with substrate2 Publications1

<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

  • fructose 6-phosphate aldolase activity Source: EcoCyc

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 functionLyase
Biological processCarbohydrate metabolism
LigandSchiff base

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G6428-MONOMER
ECOL316407:JW5109-MONOMER
MetaCyc:G6428-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P78055

<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-6-phosphate aldolase 1 (EC:4.1.2.-)
Alternative name(s):
Fructose-6-phosphate aldolase A
Short name:
FSAA
<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:fsaA
Synonyms:fsa, mipB, ybiZ
Ordered Locus Names:b0825, JW5109
<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Is an interesting tool in chemoenzymatic synthesis for the construction of chiral complex polyhydroxylated sugar-type structures. The use of hydroxyacetone (acetol) as a donor compound allows access to various 1-deoxysugars. Can also be used for the synthesis of a broad range of iminocyclitols, that are potent glycosidase and glycosyltransferase inhibitors, from dihydroxyacetone, hydroxyacetone or 1-hydroxy-butan-2-one as donor substrate, and a range of acceptor substrates.3 Publications

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>Mutagenesisi85K → R: Loss of activity. 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_00001736431 – 220Fructose-6-phosphate aldolase 1Add BLAST220

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P78055

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

More...
PaxDbi
P78055

PRoteomics IDEntifications database

More...
PRIDEi
P78055

<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

Homodecamer. Five subunits are arranged as a pentamer, and two ring-like pentamers pack like a donut to form the decamer.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4263503, 3 interactors

Database of interacting proteins

More...
DIPi
DIP-10218N

Protein interaction database and analysis system

More...
IntActi
P78055, 1 interactor

STRING: functional protein association networks

More...
STRINGi
511145.b0825

<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

1220
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
P78055

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
P78055

<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

<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 transaldolase family. Type 3A subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0176, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_079764_2_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P78055

KEGG Orthology (KO)

More...
KOi
K08313

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P78055

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00956, Transaldolase_FSA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00496, F6P_aldolase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785, Aldolase_TIM
IPR023001, F6P_aldolase
IPR001585, TAL/FSA
IPR004731, Transaldolase_3B/F6P_aldolase
IPR018225, Transaldolase_AS
IPR033919, TSA/FSA_arc/bac

The PANTHER Classification System

More...
PANTHERi
PTHR10683, PTHR10683, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00923, TAL_FSA, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00875, fsa_talC_mipB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01054, TRANSALDOLASE_1, 1 hit
PS00958, TRANSALDOLASE_2, 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.

P78055-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELYLDTSDV VAVKALSRIF PLAGVTTNPS IIAAGKKPLD VVLPQLHEAM
60 70 80 90 100
GGQGRLFAQV MATTAEGMVN DALKLRSIIA DIVVKVPVTA EGLAAIKMLK
110 120 130 140 150
AEGIPTLGTA VYGAAQGLLS ALAGAEYVAP YVNRIDAQGG SGIQTVTDLH
160 170 180 190 200
QLLKMHAPQA KVLAASFKTP RQALDCLLAG CESITLPLDV AQQMISYPAV
210 220
DAAVAKFEQD WQGAFGRTSI
Length:220
Mass (Da):22,997
Last modified:July 15, 1998 - v2
<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:i317B9A06CD19C587
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 22998 Da. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D88188 Genomic DNA Translation: BAA13552.1
U00096 Genomic DNA Translation: AAC73912.2
AP009048 Genomic DNA Translation: BAA35513.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A64820

NCBI Reference Sequences

More...
RefSeqi
NP_415346.4, NC_000913.3
WP_001336208.1, NZ_SSZK01000002.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73912; AAC73912; b0825
BAA35513; BAA35513; BAA35513

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945449

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5109
eco:b0825

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1453

<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
D88188 Genomic DNA Translation: BAA13552.1
U00096 Genomic DNA Translation: AAC73912.2
AP009048 Genomic DNA Translation: BAA35513.2
PIRiA64820
RefSeqiNP_415346.4, NC_000913.3
WP_001336208.1, NZ_SSZK01000002.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L6WX-ray1.93A/B/C/D/E/F/G/H/I/J1-220[»]
4RXFX-ray2.40A/B/C/D/E/F/G/H/I/J2-220[»]
4RXGX-ray2.15A/B/C/D/E/F/G/H/I/J1-220[»]
4RZ4X-ray1.75A/B/C/D/E/F/G/H/I/J2-220[»]
4S1FX-ray2.24A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-220[»]
5ZOLX-ray2.17A/B/C/D/E/F/G/H/I/J1-220[»]
SMRiP78055
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263503, 3 interactors
DIPiDIP-10218N
IntActiP78055, 1 interactor
STRINGi511145.b0825

Proteomic databases

jPOSTiP78055
PaxDbiP78055
PRIDEiP78055

Genome annotation databases

EnsemblBacteriaiAAC73912; AAC73912; b0825
BAA35513; BAA35513; BAA35513
GeneIDi945449
KEGGiecj:JW5109
eco:b0825
PATRICifig|1411691.4.peg.1453

Organism-specific databases

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

More...
EchoBASEi
EB3244

Phylogenomic databases

eggNOGiCOG0176, Bacteria
HOGENOMiCLU_079764_2_0_6
InParanoidiP78055
KOiK08313
PhylomeDBiP78055

Enzyme and pathway databases

BioCyciEcoCyc:G6428-MONOMER
ECOL316407:JW5109-MONOMER
MetaCyc:G6428-MONOMER
SABIO-RKiP78055

Miscellaneous databases

EvolutionaryTraceiP78055

Protein Ontology

More...
PROi
PR:P78055

Family and domain databases

CDDicd00956, Transaldolase_FSA, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00496, F6P_aldolase, 1 hit
InterProiView protein in InterPro
IPR013785, Aldolase_TIM
IPR023001, F6P_aldolase
IPR001585, TAL/FSA
IPR004731, Transaldolase_3B/F6P_aldolase
IPR018225, Transaldolase_AS
IPR033919, TSA/FSA_arc/bac
PANTHERiPTHR10683, PTHR10683, 1 hit
PfamiView protein in Pfam
PF00923, TAL_FSA, 1 hit
TIGRFAMsiTIGR00875, fsa_talC_mipB, 1 hit
PROSITEiView protein in PROSITE
PS01054, TRANSALDOLASE_1, 1 hit
PS00958, TRANSALDOLASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiFSAA_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: P78055
Secondary accession number(s): P77855, Q9R3X3
<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 15, 1998
Last sequence update: July 15, 1998
Last modified: August 12, 2020
This is version 163 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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