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Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

pheS

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

Functioni

Catalytic activityi

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per tetramer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi252 – 2521MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

  • phenylalanyl-tRNA aminoacylation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PHES-MONOMER.
ECOL316407:JW5277-MONOMER.
MetaCyc:PHES-MONOMER.
SABIO-RKP08312.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase alpha subunit (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunit
Short name:
PheRS
Gene namesi
Name:pheS
Ordered Locus Names:b1714, JW5277
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10709. pheS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
  • phenylalanine-tRNA ligase complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Phenylalanine--tRNA ligase alpha subunitPRO_0000126701Add
BLAST

Proteomic databases

EPDiP08312.
PaxDbiP08312.
PRIDEiP08312.

2D gel databases

SWISS-2DPAGEP08312.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.

Binary interactionsi

WithEntry#Exp.IntActNotes
brnQP0AD993EBI-555676,EBI-555687
erfKP391763EBI-555676,EBI-555707
pheTP073957EBI-555676,EBI-555713

Protein-protein interaction databases

BioGridi4260287. 194 interactions.
850583. 1 interaction.
DIPiDIP-6878N.
IntActiP08312. 7 interactions.
MINTiMINT-1229741.
STRINGi511145.b1714.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni15 – 2410Combined sources
Beta strandi25 – 273Combined sources
Helixi29 – 324Combined sources
Turni33 – 353Combined sources
Beta strandi36 – 416Combined sources
Turni42 – 443Combined sources
Helixi49 – 513Combined sources
Beta strandi52 – 543Combined sources
Helixi61 – 644Combined sources
Beta strandi65 – 684Combined sources
Turni69 – 735Combined sources
Helixi74 – 8512Combined sources
Turni87 – 904Combined sources
Helixi108 – 12114Combined sources
Turni122 – 1243Combined sources
Beta strandi132 – 1343Combined sources
Helixi137 – 1415Combined sources
Turni142 – 1443Combined sources
Beta strandi147 – 1493Combined sources
Helixi150 – 1545Combined sources
Beta strandi159 – 1635Combined sources
Helixi171 – 1788Combined sources
Beta strandi208 – 2158Combined sources
Helixi220 – 23516Combined sources
Beta strandi239 – 2468Combined sources
Beta strandi251 – 26010Combined sources
Beta strandi262 – 2643Combined sources
Beta strandi266 – 27510Combined sources
Helixi277 – 2815Combined sources
Turni282 – 2843Combined sources
Turni287 – 2893Combined sources
Beta strandi292 – 2987Combined sources
Helixi299 – 3079Combined sources
Helixi312 – 3154Combined sources
Helixi320 – 3245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PCOX-ray3.02A/C1-327[»]
ProteinModelPortaliP08312.
SMRiP08312. Positions 5-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CSS. Bacteria.
COG0016. LUCA.
HOGENOMiHOG000242675.
InParanoidiP08312.
KOiK01889.
OMAiKGTGWLE.
OrthoDBiEOG6WX4QN.
PhylomeDBiP08312.

Family and domain databases

HAMAPiMF_00281. Phe_tRNA_synth_alpha1.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_ligase_II_N.
IPR022911. Phe_tRNA_ligase_alpha1_bac.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR010978. tRNA-bd_arm.
[Graphical view]
PfamiPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMiSSF46589. SSF46589. 1 hit.
TIGRFAMsiTIGR00468. pheS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08312-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHLAELVAS AKAAISQASD VAALDNVRVE YLGKKGHLTL QMTTLRELPP
60 70 80 90 100
EERPAAGAVI NEAKEQVQQA LNARKAELES AALNARLAAE TIDVSLPGRR
110 120 130 140 150
IENGGLHPVT RTIDRIESFF GELGFTVATG PEIEDDYHNF DALNIPGHHP
160 170 180 190 200
ARADHDTFWF DTTRLLRTQT SGVQIRTMKA QQPPIRIIAP GRVYRNDYDQ
210 220 230 240 250
THTPMFHQME GLIVDTNISF TNLKGTLHDF LRNFFEEDLQ IRFRPSYFPF
260 270 280 290 300
TEPSAEVDVM GKNGKWLEVL GCGMVHPNVL RNVGIDPEVY SGFAFGMGME
310 320
RLTMLRYGVT DLRSFFENDL RFLKQFK
Length:327
Mass (Da):36,832
Last modified:December 1, 1992 - v2
Checksum:i601082304FD27110
GO

Sequence cautioni

The sequence CAA23564.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741R → A in CAA23564 (Ref. 2) Curated
Sequence conflicti74 – 741R → A in AAA51469 (PubMed:9278503).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981G → D in thermosensitive mutant pheS5; might cause subunit disaggregation due to electrostatic repulsion. 1 Publication
Natural varianti191 – 1911G → D Decreased affinity for Phe. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. Translation: CAA23564.1. Different initiation.
K02844 Genomic DNA. Translation: AAA51469.1.
U00096 Genomic DNA. Translation: AAC74784.1.
AP009048 Genomic DNA. Translation: BAA15482.2.
PIRiB64930. SYECFA.
RefSeqiNP_416229.1. NC_000913.3.
WP_000018596.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74784; AAC74784; b1714.
BAA15482; BAA15482; BAA15482.
GeneIDi946223.
KEGGiecj:JW5277.
eco:b1714.
PATRICi32118734. VBIEscCol129921_1785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. Translation: CAA23564.1. Different initiation.
K02844 Genomic DNA. Translation: AAA51469.1.
U00096 Genomic DNA. Translation: AAC74784.1.
AP009048 Genomic DNA. Translation: BAA15482.2.
PIRiB64930. SYECFA.
RefSeqiNP_416229.1. NC_000913.3.
WP_000018596.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PCOX-ray3.02A/C1-327[»]
ProteinModelPortaliP08312.
SMRiP08312. Positions 5-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260287. 194 interactions.
850583. 1 interaction.
DIPiDIP-6878N.
IntActiP08312. 7 interactions.
MINTiMINT-1229741.
STRINGi511145.b1714.

2D gel databases

SWISS-2DPAGEP08312.

Proteomic databases

EPDiP08312.
PaxDbiP08312.
PRIDEiP08312.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74784; AAC74784; b1714.
BAA15482; BAA15482; BAA15482.
GeneIDi946223.
KEGGiecj:JW5277.
eco:b1714.
PATRICi32118734. VBIEscCol129921_1785.

Organism-specific databases

EchoBASEiEB0703.
EcoGeneiEG10709. pheS.

Phylogenomic databases

eggNOGiENOG4105CSS. Bacteria.
COG0016. LUCA.
HOGENOMiHOG000242675.
InParanoidiP08312.
KOiK01889.
OMAiKGTGWLE.
OrthoDBiEOG6WX4QN.
PhylomeDBiP08312.

Enzyme and pathway databases

BioCyciEcoCyc:PHES-MONOMER.
ECOL316407:JW5277-MONOMER.
MetaCyc:PHES-MONOMER.
SABIO-RKP08312.

Miscellaneous databases

PROiP08312.

Family and domain databases

HAMAPiMF_00281. Phe_tRNA_synth_alpha1.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_ligase_II_N.
IPR022911. Phe_tRNA_ligase_alpha1_bac.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR010978. tRNA-bd_arm.
[Graphical view]
PfamiPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMiSSF46589. SSF46589. 1 hit.
TIGRFAMsiTIGR00468. pheS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20."
    Fayat G., Mayaux J.-F., Sacerdot C., Fromant M., Springer M., Grunberg-Manago M., Blanquet S.
    J. Mol. Biol. 171:239-261(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Miller H.I.
    Submitted (NOV-1986) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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. "Sequence of the Escherichia coli pheST operon and identification of the himA gene."
    Mechulman Y., Fayat G., Blanquet S.
    J. Bacteriol. 163:787-791(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 254-327.
  7. "Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations."
    Kast P., Hennecke H.
    J. Mol. Biol. 222:99-124(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 74, MUTAGENESIS OF ALA-294.
  8. "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.
  9. "Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases."
    Kast P., Wehrli C., Hennecke H.
    FEBS Lett. 293:160-163(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASP-191.
  10. "Identification of the pheS5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37."
    Kast P., Keller B., Hennecke H.
    J. Bacteriol. 174:1686-1689(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PHES5 ASP-98.

Entry informationi

Entry nameiSYFA_ECOLI
AccessioniPrimary (citable) accession number: P08312
Secondary accession number(s): P78233, Q59406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: December 1, 1992
Last modified: April 13, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.