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A1AUQ6

- SYE_PELPD

UniProt

A1AUQ6 - SYE_PELPD

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Pelobacter propionicus (strain DSM 2379)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

Cofactori

Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991ZincUniRule annotation
Metal bindingi101 – 1011ZincUniRule annotation
Metal bindingi126 – 1261ZincUniRule annotation
Metal bindingi128 – 1281ZincUniRule annotation
Binding sitei241 – 2411ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW
  4. tRNA binding Source: InterPro

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciPPRO338966:GHL0-3542-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:Ppro_3484
OrganismiPelobacter propionicus (strain DSM 2379)
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
ProteomesiUP000006732: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Glutamate--tRNA ligasePRO_1000001930Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi338966.Ppro_3484.

Structurei

3D structure databases

ProteinModelPortaliA1AUQ6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi10 – 2011"HIGH" regionAdd
BLAST
Motifi238 – 2425"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
OMAiDSHEHHA.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1AUQ6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDIRVRFAP SPTGYLHVGG ARTALFNWLL ARKQGGTFIL RIEDTDVERS
60 70 80 90 100
TQESVDAILQ GMEWLGLDWD EGPFYQTDNF PLYREYIQKL LDEGKAYRCY
110 120 130 140 150
CTAEELEAKR ELAMKEGRKP KYDGTCRDLT EQPADRPFVV RFRAPQDGGA
160 170 180 190 200
TSFNDLIKGT ITFPNDELDD LIVQRSDGTP TYNFCVVIDD AIMKITTVIR
210 220 230 240 250
GDDHVNNTPR QVQLYQALGF PVPQFAHVPM ILGSDKARLS KRHGATSVIA
260 270 280 290 300
YRDMGFLPEA LMNYLVRLGW SHGDDEIFSR DEMVAKFDIS NVGRSPSVFN
310 320 330 340 350
PDKLLWLNAH YIKHGDPQRL ADLLVPFLKM RGVDPANGGP QLAVAIKTLQ
360 370 380 390 400
ERARTMLEMA DSALFYYHAP ESYDRTALAK FEKEHLLAVY ATVAEKLSAA
410 420 430 440 450
TAVTAAEFDA LFKEICAEKG WKMPQVGQPV RIALSGGTHA PGIGEIIVTL
460
GKEETIQRIQ RAREFVEKQ
Length:469
Mass (Da):52,729
Last modified:January 23, 2007 - v1
Checksum:i94493BD6C9EFF23B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000482 Genomic DNA. Translation: ABL01077.1.
RefSeqiYP_903134.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABL01077; ABL01077; Ppro_3484.
GeneIDi4572651.
KEGGippd:Ppro_3484.
PATRICi22900113. VBIPelPro64470_3642.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000482 Genomic DNA. Translation: ABL01077.1 .
RefSeqi YP_903134.1. NC_008609.1.

3D structure databases

ProteinModelPortali A1AUQ6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 338966.Ppro_3484.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL01077 ; ABL01077 ; Ppro_3484 .
GeneIDi 4572651.
KEGGi ppd:Ppro_3484.
PATRICi 22900113. VBIPelPro64470_3642.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252722.
KOi K01885.
OMAi DSHEHHA.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci PPRO338966:GHL0-3542-MONOMER.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. 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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF48163. SSF48163. 1 hit.
TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2379.

Entry informationi

Entry nameiSYE_PELPD
AccessioniPrimary (citable) accession number: A1AUQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 57 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

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3