Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0C1A6 (SYE1_HYPNA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:HNE_1783
OrganismHyphomonas neptunium (strain ATCC 15444) [Complete proteome] [HAMAP]
Taxonomic identifier228405 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeHyphomonas

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367691

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0C1A6 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 29EB8DAC026742F2

FASTA48653,324
        10         20         30         40         50         60 
MSVVTRFAPS PTGMLHIGGA RTALFNYLFA RRNGGRFLLR IEDTDRERST QEATDAILDA 

        70         80         90        100        110        120 
MEWLGLTPDE PPVMQSAQVD RHAAVAHDMV ARGTAFRCYV TPEELQARRD LGEEKRQAAK 

       130        140        150        160        170        180 
QEGISDAEKE ALLAEASQLL APFRSPYRDG ASPPSPDAPF TVRLRAPESG PRTVEDGVQG 

       190        200        210        220        230        240 
TVTIDASEID DLVMLRADGT PTYMLAVVVD DHDMGITHVI RGDDHLRNTF RQVPIYEAMG 

       250        260        270        280        290        300 
WSVPNFSHVP MIHGNDGAKL SKRHGALSTT AYRDMGYLPE AMKAYLLRLG WSHGDQEIFT 

       310        320        330        340        350        360 
DEEAVQVFDV SGINKAPARL DLDKLATVNA HFMRLAADER LFDLICPVLS KNCSLSDAEV 

       370        380        390        400        410        420 
ARIRAALPHM KDRGSTLIEL ANAFAFLYAK RPLELNKNAV KALSDEGKLR LKGLYDDLQR 

       430        440        450        460        470        480 
MSQWSGASIS ETIKSYCAAT GLSMGQIGPP LRAALTGGLP APDLAPVMDW LGREETLARI 


DDQLAG 

« Hide

References

[1]"Comparative genomic evidence for a close relationship between the dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter crescentus."
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., Brinkac L.M. expand/collapse author list , Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., Ward N.L.
J. Bacteriol. 188:6841-6850(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15444.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000158 Genomic DNA. Translation: ABI77242.1.
RefSeqYP_760487.1. NC_008358.1.

3D structure databases

ProteinModelPortalQ0C1A6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228405.HNE_1783.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI77242; ABI77242; HNE_1783.
GeneID4289642.
KEGGhne:HNE_1783.
PATRIC32216395. VBIHypNep17450_1786.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycHNEP228405:GI69-1783-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_HYPNA
AccessionPrimary (citable) accession number: Q0C1A6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries