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B2IYI1 (SYE_NOSP7) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 39. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:Npun_R1357
OrganismNostoc punctiforme (strain ATCC 29133 / PCC 73102) [Complete proteome] [HAMAP]
Taxonomic identifier63737 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length481 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.

Sequence caution

The sequence ACC80068.1 differs from that shown. Reason: Erroneous initiation.

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 – 481481Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367721

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif247 – 2515"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2501ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2IYI1 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 9AF27CA5C6F9CCC6

FASTA48154,437
        10         20         30         40         50         60 
MTVRVRIAPS PTGNLHIGTA RTAVFNWLFA RHHGGKFILR IEDTDLERSR PEYTDNILEG 

        70         80         90        100        110        120 
LRWLGLNWDE GPFFQSQRLD LYKEAVQKLL DQGLAYRCYT TSEELEALRE AQKARGEAPR 

       130        140        150        160        170        180 
YDNRHRNLTP EQRAAYEAEG RSYVIRFKIE DGREIVWNDL VRGKMSWRGS DLGGDMVIAR 

       190        200        210        220        230        240 
ASEEGSGQPL YNFVVVVDDI DMQITHVIRG EDHIANTAKQ ILLYEAMGAK IPEFSHTPLI 

       250        260        270        280        290        300 
LNMEGRKLSK RDGVTSISEF QKMGFTAEGL VNYMTLLGWS PPDSTQEIFT LETAAKEFGF 

       310        320        330        340        350        360 
ERVNKAGAKF DWDKLDWLNS QYIHNTPVDK LTDLLIPFWE AAGYKFDGGR DRAWLEQLVT 

       370        380        390        400        410        420 
LISQSLTRLV DAVPQSQLFF SDTVEFSEEG STQLKQEGST AVLEAIVTAL ENQPQLSEAA 

       430        440        450        460        470        480 
AQDIIKQVVK EQKVKKGLVM RSLRAALTGD VHGPDLIQSW LLLNQIGLDK SRLSRAITEA 


N 

« Hide

References

[1]"Complete sequence of chromosome of Nostoc punctiforme ATCC 29133."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C. expand/collapse author list , Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29133 / PCC 73102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001037 Genomic DNA. Translation: ACC80068.1. Different initiation.
RefSeqYP_001865011.1. NC_010628.1.

3D structure databases

ProteinModelPortalB2IYI1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING63737.Npun_R1357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC80068; ACC80068; Npun_R1357.
GeneID6250810.
KEGGnpu:Npun_R1357.
PATRIC22754697. VBINosPun48114_1551.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.
PhylomeDBB2IYI1.

Enzyme and pathway databases

BioCycNPUN63737:GJNP-1334-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 nameSYE_NOSP7
AccessionPrimary (citable) accession number: B2IYI1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: July 9, 2014
This is version 39 of the entry and version 2 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