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Protein

Enterobactin synthase component B

Gene

entB

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

Functioni

Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron2+ atoms. EntB is a bifunctional protein that serves as an isochorismate lyase and an aryl carrier protein (ArCP). Catalyzes the conversion of isochorismate to 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), the precursor of 2,3-dihydroxybenzoate (DHB). In the enterobactin assembly, EntB functions as an aryl carrier protein phosphopantetheinylated near the C terminus by EntD to yield holo-EntB, which is then acylated by EntE with 2,3-dihydroxybenzoyl-AMP to form DHB-holo-EntB. Then this product will serve in the formation of the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine.8 Publications

Catalytic activityi

6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate.4 Publications
Isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate.4 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by 3-[(carboxyethenyl)oxy]-6-hydroxy-1-benzoic acid and 3-[(carboxyethenyl)oxy]benzoic acid.1 Publication

Kineticsi

Kcat is 600 min(-1) for isochorismatase activity with isochorismate as substrate (at pH 7 and 37 degrees Celsius). Kcat is 540 min(-1) for isochorismatase activity with 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate as substrate (at pH 7 and 37 degrees Celsius). Kcat is 310 min(-1) for isochorismatase activity with 4,5-dihydroisochorismate as substrate (at pH 7 and 37 degrees Celsius).1 Publication

  1. KM=14.7 µM for isochorismate (at pH 7 and 37 degrees Celsius)1 Publication
  2. KM=23 µM for 4,5-dihydroisochorismate (at pH 7 and 37 degrees Celsius)1 Publication
  3. KM=86 µM for 3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid (at pH 7 and 37 degrees Celsius)1 Publication
  4. KM=120 µM for 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate (at pH 7 and 37 degrees Celsius)1 Publication
  5. KM=280 µM for cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid (at pH 7 and 37 degrees Celsius)1 Publication
  1. Vmax=18.5 µmol/min/mg enzyme (at pH 7 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 6.5 and 7.5. At pH 5.5, EntB retains 50% of isochorismatase activity.1 Publication

Pathwayi: enterobactin biosynthesis

This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi227 – 2271Magnesium1 Publication
Metal bindingi242 – 2421Magnesium; via carbonyl oxygen1 Publication
Metal bindingi244 – 2441Magnesium1 Publication

GO - Molecular functioni

  • 2,3-dihydroxybenzoate-serine ligase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • isochorismatase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • phosphopantetheine binding Source: UniProtKB
  • transferase activity, transferring alkyl or aryl (other than methyl) groups Source: EcoliWiki

GO - Biological processi

  • enterobactin biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase

Keywords - Biological processi

Enterobactin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:ENTB-MONOMER.
ECOL316407:JW0587-MONOMER.
MetaCyc:ENTB-MONOMER.
BRENDAi3.3.2.1. 2026.
6.3.2.14. 2026.
SABIO-RKP0ADI4.
UniPathwayiUPA00017.

Names & Taxonomyi

Protein namesi
Recommended name:
Enterobactin synthase component B1 Publication (EC:6.3.2.144 Publications)
Alternative name(s):
Enterobactin biosynthesis bifunctional protein EntB1 Publication
Enterochelin synthase B1 Publication
Including the following 2 domains:
Isochorismatase1 Publication (EC:3.3.2.14 Publications)
Alternative name(s):
2,3-dihydro-2,3-dihydroxybenzoate synthase1 Publication
Isochorismate lyase1 Publication
Aryl carrier protein1 Publication
Short name:
ArCP1 Publication
Gene namesi
Name:entB1 Publication
Synonyms:entG1 Publication
Ordered Locus Names:b0595, JW0587
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10260. entB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are hypersensitive to the antimicrobial peptide wrwycr.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi240 – 2401D → R: The catalytic efficiency slightly increases, but a 8-fold decrease of the affinity for the S-dihydroxybenzoyltransferase EntE is observed. 1 Publication
Mutagenesisi242 – 2421G → A: Not efficiently phosphopantetheinylated by EntD. 1 Publication
Mutagenesisi244 – 2441D → A: Efficiently phosphopantetheinylated by EntD. 1 Publication
Mutagenesisi244 – 2441D → R: Not efficiently phosphopantetheinylated by EntD. 1 Publication
Mutagenesisi249 – 2491M → A: Unable to recognize EntE and EntF. Exhibits a decrease in the enterobactin production compared to the wild-type. Still able to be phosphopantetheinylated. 1 Publication
Mutagenesisi263 – 2631D → R: The catalytic efficiency is the same as the wild-type, but a 3-fold decrease of the affinity for the S-dihydroxybenzoyltransferase EntE is observed. 1 Publication
Mutagenesisi264 – 2641F → E: The affinity for EntE and catalytic efficiency of the S-dihydroxybenzoyltransferase EntE are below that of the wild-type. 2 Publications
Mutagenesisi268 – 2681A → Q: Unable to recognize EntE and EntF. Exhibits a decrease in the enterobactin production compared to the wild-type. Still able to be phosphopantetheinylated. 1 Publication
Mutagenesisi269 – 2691K → A: Behaves similarly to the wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 285284Enterobactin synthase component BPRO_0000201822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei245 – 2451O-(pantetheine 4'-phosphoryl)serine1 Publication

Post-translational modificationi

4'-phosphopantetheine is transferred from CoA to a specific serine of apo-EntB by EntD. Holo-EntB so formed is then acylated with 2,3-dihydroxybenzoate in a reaction catalyzed by EntE.1 Publication

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

EPDiP0ADI4.
PaxDbiP0ADI4.
PRIDEiP0ADI4.

2D gel databases

SWISS-2DPAGEP0ADI4.

Expressioni

Inductioni

Under conditions of iron deficiency and by the fur protein.1 Publication

Interactioni

Subunit structurei

Proteins EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase. Dimer.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-547993,EBI-547993
entHP0A8Y83EBI-547993,EBI-1118982

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4260905. 198 interactions.
DIPiDIP-9512N.
IntActiP0ADI4. 29 interactions.
MINTiMINT-1241343.
STRINGi511145.b0595.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Helixi28 – 303Combined sources
Beta strandi31 – 366Combined sources
Helixi40 – 434Combined sources
Helixi51 – 6919Combined sources
Beta strandi74 – 785Combined sources
Helixi85 – 884Combined sources
Helixi91 – 955Combined sources
Helixi98 – 1014Combined sources
Helixi103 – 1053Combined sources
Helixi110 – 1123Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi125 – 1273Combined sources
Turni128 – 1314Combined sources
Helixi134 – 1407Combined sources
Beta strandi145 – 1517Combined sources
Turni153 – 1553Combined sources
Helixi156 – 16611Combined sources
Beta strandi170 – 17910Combined sources
Helixi183 – 19614Combined sources
Beta strandi199 – 2013Combined sources
Helixi203 – 2064Combined sources
Beta strandi207 – 2093Combined sources
Helixi215 – 2228Combined sources
Helixi223 – 2253Combined sources
Helixi239 – 2413Combined sources
Helixi247 – 2559Combined sources
Turni256 – 2583Combined sources
Helixi264 – 2685Combined sources
Helixi273 – 2819Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FQ1X-ray2.30A/B1-285[»]
3RG2X-ray3.10A/B/C/D/E/F/G/H/I/J209-285[»]
ProteinModelPortaliP0ADI4.
SMRiP0ADI4. Positions 4-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADI4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 28168Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 213212Isochorismatase1 PublicationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the isochorismatase family.Curated
Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105WQI. Bacteria.
COG1535. LUCA.
COG3433. LUCA.
HOGENOMiHOG000078667.
InParanoidiP0ADI4.
KOiK01252.
OMAiRDIKPFF.
OrthoDBiEOG6G20K9.
PhylomeDBiP0ADI4.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.850. 1 hit.
InterProiIPR016291. Isochorismatase.
IPR000868. Isochorismatase-like.
IPR009081. PP-bd_ACP.
[Graphical view]
PfamiPF00857. Isochorismatase. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF001111. Isochorismatase. 1 hit.
PRINTSiPR01398. ISCHRISMTASE.
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF52499. SSF52499. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ADI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIPKLQAYA LPESHDIPQN KVDWAFEPQR AALLIHDMQD YFVSFWGENC
60 70 80 90 100
PMMEQVIANI AALRDYCKQH NIPVYYTAQP KEQSDEDRAL LNDMWGPGLT
110 120 130 140 150
RSPEQQKVVD RLTPDADDTV LVKWRYSAFH RSPLEQMLKE SGRNQLIITG
160 170 180 190 200
VYAHIGCMTT ATDAFMRDIK PFMVADALAD FSRDEHLMSL KYVAGRSGRV
210 220 230 240 250
VMTEELLPAP IPASKAALRE VILPLLDESD EPFDDDNLID YGLDSVRMMA
260 270 280
LAARWRKVHG DIDFVMLAKN PTIDAWWKLL SREVK
Length:285
Mass (Da):32,554
Last modified:December 6, 2005 - v1
Checksum:iE98C62D5ED23BAB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24148 Unassigned DNA. Translation: AAA16102.1.
M24143 Genomic DNA. Translation: AAA76835.1.
U82598 Genomic DNA. Translation: AAB40795.1.
U00096 Genomic DNA. Translation: AAC73696.1.
AP009048 Genomic DNA. Translation: BAE76350.1.
PIRiC91904. YXECIC.
RefSeqiNP_415127.1. NC_000913.3.
WP_001007138.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73696; AAC73696; b0595.
BAE76350; BAE76350; BAE76350.
GeneIDi946178.
KEGGiecj:JW0587.
eco:b0595.
PATRICi32116366. VBIEscCol129921_0623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24148 Unassigned DNA. Translation: AAA16102.1.
M24143 Genomic DNA. Translation: AAA76835.1.
U82598 Genomic DNA. Translation: AAB40795.1.
U00096 Genomic DNA. Translation: AAC73696.1.
AP009048 Genomic DNA. Translation: BAE76350.1.
PIRiC91904. YXECIC.
RefSeqiNP_415127.1. NC_000913.3.
WP_001007138.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FQ1X-ray2.30A/B1-285[»]
3RG2X-ray3.10A/B/C/D/E/F/G/H/I/J209-285[»]
ProteinModelPortaliP0ADI4.
SMRiP0ADI4. Positions 4-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260905. 198 interactions.
DIPiDIP-9512N.
IntActiP0ADI4. 29 interactions.
MINTiMINT-1241343.
STRINGi511145.b0595.

2D gel databases

SWISS-2DPAGEP0ADI4.

Proteomic databases

EPDiP0ADI4.
PaxDbiP0ADI4.
PRIDEiP0ADI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73696; AAC73696; b0595.
BAE76350; BAE76350; BAE76350.
GeneIDi946178.
KEGGiecj:JW0587.
eco:b0595.
PATRICi32116366. VBIEscCol129921_0623.

Organism-specific databases

EchoBASEiEB0256.
EcoGeneiEG10260. entB.

Phylogenomic databases

eggNOGiENOG4105WQI. Bacteria.
COG1535. LUCA.
COG3433. LUCA.
HOGENOMiHOG000078667.
InParanoidiP0ADI4.
KOiK01252.
OMAiRDIKPFF.
OrthoDBiEOG6G20K9.
PhylomeDBiP0ADI4.

Enzyme and pathway databases

UniPathwayiUPA00017.
BioCyciEcoCyc:ENTB-MONOMER.
ECOL316407:JW0587-MONOMER.
MetaCyc:ENTB-MONOMER.
BRENDAi3.3.2.1. 2026.
6.3.2.14. 2026.
SABIO-RKP0ADI4.

Miscellaneous databases

EvolutionaryTraceiP0ADI4.
PROiP0ADI4.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.850. 1 hit.
InterProiIPR016291. Isochorismatase.
IPR000868. Isochorismatase-like.
IPR009081. PP-bd_ACP.
[Graphical view]
PfamiPF00857. Isochorismatase. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF001111. Isochorismatase. 1 hit.
PRINTSiPR01398. ISCHRISMTASE.
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF52499. SSF52499. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and transcriptional organization of the Escherichia coli enterobactin biosynthesis cistrons entB and entA."
    Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.
    J. Bacteriol. 171:784-790(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
  2. "Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase."
    Liu J., Duncan K., Walsh C.T.
    J. Bacteriol. 171:791-798(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase."
    Rusnak F., Liu J., Quinn N., Berchtold G.A., Walsh C.T.
    Biochemistry 29:1425-1435(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
  7. "Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product."
    Rusnak F., Faraci W.S., Walsh C.T.
    Biochemistry 28:6827-6835(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "EntG activity of Escherichia coli enterobactin synthetase."
    Staab J.F., Earhart C.F.
    J. Bacteriol. 172:6403-6410(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate."
    Gehring A.M., Bradley K.A., Walsh C.T.
    Biochemistry 36:8495-8503(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  10. "Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF."
    Gehring A.M., Mori I., Walsh C.T.
    Biochemistry 37:2648-2659(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  11. "Membrane association of the Escherichia coli enterobactin synthase proteins EntB/G, EntE, and EntF."
    Hantash F.M., Earhart C.F.
    J. Bacteriol. 182:1768-1773(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Localized protein interaction surfaces on the EntB carrier protein revealed by combinatorial mutagenesis and selection."
    Lai J.R., Fischbach M.A., Liu D.R., Walsh C.T.
    J. Am. Chem. Soc. 128:11002-11003(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-242 AND ASP-244.
  13. "A protein interaction surface in nonribosomal peptide synthesis mapped by combinatorial mutagenesis and selection."
    Lai J.R., Fischbach M.A., Liu D.R., Walsh C.T.
    Proc. Natl. Acad. Sci. U.S.A. 103:5314-5319(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF MET-249; PHE-264; ALA-268 AND LYS-269.
  14. "Ligand-induced conformational rearrangements promote interaction between the Escherichia coli enterobactin biosynthetic proteins EntE and EntB."
    Khalil S., Pawelek P.D.
    J. Mol. Biol. 393:658-671(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Escherichia coli enterobactin synthesis and uptake mutants are hypersensitive to an antimicrobial peptide that limits the availability of iron in addition to blocking Holliday junction resolution."
    Orchard S.S., Rostron J.E., Segall A.M.
    Microbiology 158:547-559(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  16. "Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain."
    Drake E.J., Nicolai D.A., Gulick A.M.
    Chem. Biol. 13:409-419(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-240; ASP-263 AND PHE-264, COFACTOR, SUBUNIT.
  17. "Structural and functional investigation of the intermolecular interaction between NRPS adenylation and carrier protein domains."
    Sundlov J.A., Shi C., Wilson D.J., Aldrich C.C., Gulick A.M.
    Chem. Biol. 19:188-198(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 209-285 IN A CHIMERIC CONSTRUCT WITH ENTE IN COMPLEX WITH PHOSPHOPANTETHEINE, SUBUNIT, PHOSPHOPANTETHEINYLATION AT SER-245.

Entry informationi

Entry nameiENTB_ECOLI
AccessioniPrimary (citable) accession number: P0ADI4
Secondary accession number(s): P15048, Q2MBK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: May 11, 2016
This is version 94 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, Multifunctional enzyme, 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.