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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)DescriptionActionsGraphical viewLength
Metal bindingi252MagnesiumBy similarity1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001267011 – 327Phenylalanine--tRNA ligase alpha subunitAdd BLAST327

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 interactors.
850583. 1 interactor.
DIPiDIP-6878N.
IntActiP08312. 7 interactors.
MINTiMINT-1229741.
STRINGi511145.b1714.

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni15 – 24Combined sources10
Beta strandi25 – 27Combined sources3
Helixi29 – 32Combined sources4
Turni33 – 35Combined sources3
Beta strandi36 – 41Combined sources6
Turni42 – 44Combined sources3
Helixi49 – 51Combined sources3
Beta strandi52 – 54Combined sources3
Helixi61 – 64Combined sources4
Beta strandi65 – 68Combined sources4
Turni69 – 73Combined sources5
Helixi74 – 85Combined sources12
Turni87 – 90Combined sources4
Helixi108 – 121Combined sources14
Turni122 – 124Combined sources3
Beta strandi132 – 134Combined sources3
Helixi137 – 141Combined sources5
Turni142 – 144Combined sources3
Beta strandi147 – 149Combined sources3
Helixi150 – 154Combined sources5
Beta strandi159 – 163Combined sources5
Helixi171 – 178Combined sources8
Beta strandi208 – 215Combined sources8
Helixi220 – 235Combined sources16
Beta strandi239 – 246Combined sources8
Beta strandi251 – 260Combined sources10
Beta strandi262 – 264Combined sources3
Beta strandi266 – 275Combined sources10
Helixi277 – 281Combined sources5
Turni282 – 284Combined sources3
Turni287 – 289Combined sources3
Beta strandi292 – 298Combined sources7
Helixi299 – 307Combined sources9
Helixi312 – 315Combined sources4
Helixi320 – 324Combined sources5

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CSS. Bacteria.
COG0016. LUCA.
HOGENOMiHOG000242675.
InParanoidiP08312.
KOiK01889.
OMAiEYHPARD.
PhylomeDBiP08312.

Family and domain databases

HAMAPiMF_00281. Phe_tRNA_synth_alpha1. 1 hit.
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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74R → A in CAA23564 (Ref. 2) Curated1
Sequence conflicti74R → A in AAA51469 (PubMed:9278503).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti98G → D in thermosensitive mutant pheS5; might cause subunit disaggregation due to electrostatic repulsion. 1 Publication1
Natural varianti191G → D Decreased affinity for Phe. 1 Publication1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PCOX-ray3.02A/C1-327[»]
ProteinModelPortaliP08312.
SMRiP08312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260287. 194 interactors.
850583. 1 interactor.
DIPiDIP-6878N.
IntActiP08312. 7 interactors.
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.
OMAiEYHPARD.
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. 1 hit.
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...

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: November 2, 2016
This is version 160 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.