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Protein

Adenylate kinase

Gene

adk

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

Functioni

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.UniRule annotation2 Publications

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation1 Publication

Kineticsi

  1. KM=51 µM for ATP (at pH 7.4 and 30 degrees Celsius)1 Publication
  2. KM=38 µM for AMP (at pH 7.4 and 30 degrees Celsius)1 Publication
  3. KM=92 µM for ADP (at pH 7.4 and 30 degrees Celsius)1 Publication
  1. Vmax=1020 µmol/min/mg enzyme for the forward reaction (at pH 7.4 and 30 degrees Celsius)1 Publication
  2. Vmax=605 µmol/min/mg enzyme for the reverse reaction (at pH 7.4 and 30 degrees Celsius)1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius. Thermostable. Is half-inactivated at 52 degrees Celsius.1 Publication

Pathwayi: AMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from ADP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Adenylate kinase (adk)
This subpathway is part of the pathway AMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from ADP, the pathway AMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311AMPUniRule annotation5 Publications
Binding sitei36 – 361AMPUniRule annotation5 Publications
Binding sitei92 – 921AMPUniRule annotation5 Publications
Binding sitei119 – 1191ATP1 Publication
Binding sitei123 – 1231ATPUniRule annotation5 Publications
Binding sitei156 – 1561AMPUniRule annotation5 Publications
Binding sitei167 – 1671AMPUniRule annotation3 Publications
Binding sitei200 – 2001ATP; via carbonyl oxygenUniRule annotation5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156ATPUniRule annotation5 Publications
Nucleotide bindingi57 – 593AMPUniRule annotation5 Publications
Nucleotide bindingi85 – 884AMPUniRule annotation3 Publications
Nucleotide bindingi132 – 1332ATPUniRule annotation4 Publications

GO - Molecular functioni

  • adenylate kinase activity Source: EcoCyc
  • AMP binding Source: EcoCyc
  • ATP binding Source: EcoCyc
  • magnesium ion binding Source: EcoCyc

GO - Biological processi

  • ADP biosynthetic process Source: EcoliWiki
  • AMP salvage Source: UniProtKB-UniPathway
  • nucleotide phosphorylation Source: GOC
  • phospholipid biosynthetic process Source: EcoliWiki
  • purine ribonucleotide interconversion Source: EcoCyc
  • RNA biosynthetic process Source: EcoliWiki
  • translation Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ADENYL-KIN-MONOMER.
ECOL316407:JW0463-MONOMER.
MetaCyc:ADENYL-KIN-MONOMER.
BRENDAi2.7.4.3. 2026.
SABIO-RKP69441.
UniPathwayiUPA00588; UER00649.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinaseUniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AKUniRule annotation
Alternative name(s):
ATP-AMP transphosphorylaseUniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Gene namesi
Name:adkUniRule annotation
Synonyms:dnaW, plsA
Ordered Locus Names:b0474, JW0463
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10032. adk.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91P → G: No loss of enzyme activity. 2 Publications
Mutagenesisi10 – 101G → V: No loss of enzyme activity. 3 Publications
Mutagenesisi13 – 131K → Q: Drastic reduction in enzyme activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 214214Adenylate kinasePRO_0000158767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP69441.
PaxDbiP69441.
PRIDEiP69441.

2D gel databases

SWISS-2DPAGEP69441.

Interactioni

Subunit structurei

Monomer.UniRule annotation3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ybdLP778062EBI-543592,EBI-543661

Protein-protein interaction databases

BioGridi4261613. 11 interactions.
DIPiDIP-47903N.
IntActiP69441. 13 interactions.
STRINGi511145.b0474.

Structurei

Secondary structure

1
214
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi13 – 2412Combined sources
Beta strandi28 – 303Combined sources
Helixi31 – 4111Combined sources
Turni44 – 463Combined sources
Helixi47 – 493Combined sources
Helixi50 – 556Combined sources
Helixi61 – 7212Combined sources
Helixi75 – 773Combined sources
Beta strandi81 – 855Combined sources
Helixi90 – 9910Combined sources
Beta strandi104 – 1107Combined sources
Helixi113 – 1153Combined sources
Helixi116 – 1205Combined sources
Beta strandi123 – 1253Combined sources
Turni127 – 1293Combined sources
Beta strandi132 – 1343Combined sources
Turni135 – 1373Combined sources
Turni147 – 1493Combined sources
Helixi157 – 1593Combined sources
Helixi161 – 17414Combined sources
Turni175 – 1773Combined sources
Helixi178 – 18710Combined sources
Beta strandi190 – 1978Combined sources
Helixi202 – 21312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKEX-ray2.00A/B1-214[»]
1ANKX-ray2.00A/B1-214[»]
1E4VX-ray1.85A/B1-214[»]
1E4YX-ray1.85A/B1-214[»]
2ECKX-ray2.80A/B1-214[»]
3HPQX-ray2.00A/B1-214[»]
3HPRX-ray2.00A/B1-214[»]
4AKEX-ray2.20A/B1-214[»]
4X8HX-ray2.50A1-214[»]
4X8LX-ray1.70A/B1-214[»]
4X8MX-ray2.60A1-214[»]
4X8OX-ray2.10A/B1-214[»]
ProteinModelPortaliP69441.
SMRiP69441. Positions 1-214.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69441.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5930NMPbindUniRule annotation1 PublicationAdd
BLAST
Regioni122 – 15938LIDUniRule annotation1 PublicationAdd
BLAST

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CC8. Bacteria.
COG0563. LUCA.
HOGENOMiHOG000238772.
InParanoidiP69441.
KOiK00939.
OMAiRVYHIVF.
OrthoDBiEOG679TH4.
PhylomeDBiP69441.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P69441-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIILLGAPG AGKGTQAQFI MEKYGIPQIS TGDMLRAAVK SGSELGKQAK
60 70 80 90 100
DIMDAGKLVT DELVIALVKE RIAQEDCRNG FLLDGFPRTI PQADAMKEAG
110 120 130 140 150
INVDYVLEFD VPDELIVDRI VGRRVHAPSG RVYHVKFNPP KVEGKDDVTG
160 170 180 190 200
EELTTRKDDQ EETVRKRLVE YHQMTAPLIG YYSKEAEAGN TKYAKVDGTK
210
PVAEVRADLE KILG
Length:214
Mass (Da):23,586
Last modified:August 13, 1987 - v1
Checksum:iBB917C84000A80EE
GO

Sequence cautioni

The sequence AAB40228.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03038 Genomic DNA. Translation: CAA26840.1.
U82664 Genomic DNA. Translation: AAB40228.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73576.1.
AP009048 Genomic DNA. Translation: BAE76253.1.
M38777 Genomic DNA. Translation: AAA23461.1.
D90259 Genomic DNA. Translation: BAA14303.1.
PIRiA24275. KIECA.
RefSeqiNP_415007.1. NC_000913.3.
WP_001220233.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73576; AAC73576; b0474.
BAE76253; BAE76253; BAE76253.
GeneIDi945097.
KEGGiecj:JW0463.
eco:b0474.
PATRICi32116105. VBIEscCol129921_0494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03038 Genomic DNA. Translation: CAA26840.1.
U82664 Genomic DNA. Translation: AAB40228.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73576.1.
AP009048 Genomic DNA. Translation: BAE76253.1.
M38777 Genomic DNA. Translation: AAA23461.1.
D90259 Genomic DNA. Translation: BAA14303.1.
PIRiA24275. KIECA.
RefSeqiNP_415007.1. NC_000913.3.
WP_001220233.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKEX-ray2.00A/B1-214[»]
1ANKX-ray2.00A/B1-214[»]
1E4VX-ray1.85A/B1-214[»]
1E4YX-ray1.85A/B1-214[»]
2ECKX-ray2.80A/B1-214[»]
3HPQX-ray2.00A/B1-214[»]
3HPRX-ray2.00A/B1-214[»]
4AKEX-ray2.20A/B1-214[»]
4X8HX-ray2.50A1-214[»]
4X8LX-ray1.70A/B1-214[»]
4X8MX-ray2.60A1-214[»]
4X8OX-ray2.10A/B1-214[»]
ProteinModelPortaliP69441.
SMRiP69441. Positions 1-214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261613. 11 interactions.
DIPiDIP-47903N.
IntActiP69441. 13 interactions.
STRINGi511145.b0474.

2D gel databases

SWISS-2DPAGEP69441.

Proteomic databases

EPDiP69441.
PaxDbiP69441.
PRIDEiP69441.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73576; AAC73576; b0474.
BAE76253; BAE76253; BAE76253.
GeneIDi945097.
KEGGiecj:JW0463.
eco:b0474.
PATRICi32116105. VBIEscCol129921_0494.

Organism-specific databases

EchoBASEiEB0031.
EcoGeneiEG10032. adk.

Phylogenomic databases

eggNOGiENOG4105CC8. Bacteria.
COG0563. LUCA.
HOGENOMiHOG000238772.
InParanoidiP69441.
KOiK00939.
OMAiRVYHIVF.
OrthoDBiEOG679TH4.
PhylomeDBiP69441.

Enzyme and pathway databases

UniPathwayiUPA00588; UER00649.
BioCyciEcoCyc:ADENYL-KIN-MONOMER.
ECOL316407:JW0463-MONOMER.
MetaCyc:ADENYL-KIN-MONOMER.
BRENDAi2.7.4.3. 2026.
SABIO-RKP69441.

Miscellaneous databases

EvolutionaryTraceiP69441.
PROiP69441.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli."
    Brune M., Schumann R., Wittinghofer F.
    Nucleic Acids Res. 13:7139-7151(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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. "Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli."
    Bardwell J.C.A., Craig E.A.
    Proc. Natl. Acad. Sci. U.S.A. 84:5177-5181(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
  6. "Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12."
    Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.
    J. Mol. Biol. 219:393-398(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-214.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  8. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. Cited for: PROTEIN SEQUENCE OF 1-4.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Role of adenylate kinase in the regulation of macromolecular biosynthesis in a putative mutant of Escherichia coli defective in membrane phospholipid biosynthesis."
    Glaser M., Nulty W., Vagelos P.R.
    J. Bacteriol. 123:128-136(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Genetic analysis of Escherichia coli mutants defective in adenylate kinase and sn-glycerol 3-phosphate acyltransferase."
    Esmon B.E., Kensil C.R., Cheng C.H., Glaser M.
    J. Bacteriol. 141:405-408(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli."
    Reinstein J., Brune M., Wittinghofer A.
    Biochemistry 27:4712-4720(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-10 AND LYS-13.
  13. "Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli."
    Reinstein J., Schlichting I., Wittinghofer A.
    Biochemistry 29:7451-7459(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-9; GLY-10 AND LYS-13.
  14. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  15. "A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: a predictive and experimental study."
    Munier-Lehmann H., Burlacu-Miron S., Craescu C.T., Mantsch H.H., Schultz C.P.
    Proteins 36:238-248(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  16. "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-192, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  17. "Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9-A resolution. A model for a catalytic transition state."
    Mueller C.W., Schulz G.E.
    J. Mol. Biol. 224:159-177(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH THE INHIBITOR AP5A.
  18. "Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop."
    Mueller C.W., Schulz G.E.
    Proteins 15:42-49(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS PRO-9 AND GLY-10 IN COMPLEX WITH THE INHIBITOR AP5A.
  19. "The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP."
    Berry M.B., Meador B., Bilderback T., Liang P., Glaser M., Phillips G.N. Jr.
    Proteins 19:183-198(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH AMP AND AMPPNP.
  20. "Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding."
    Mueller C.W., Schlauderer G.J., Reinstein J., Schulz G.E.
    Structure 4:147-156(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    Strain: K12.
  21. "Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase."
    Berry M.B., Bae E., Bilderback T.R., Glaser M., Phillips G.N. Jr.
    Proteins 62:555-556(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ADP AND AMP.
  22. "Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins."
    Schrank T.P., Bolen D.W., Hilser V.J.
    Proc. Natl. Acad. Sci. U.S.A. 106:16984-16989(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP5A.

Entry informationi

Entry nameiKAD_ECOLI
AccessioniPrimary (citable) accession number: P69441
Secondary accession number(s): P05082, P77123, Q2MBV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: March 16, 2016
This is version 114 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, Direct protein sequencing, 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

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.