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A7FSY9

- SYE_CLOB1

UniProt

A7FSY9 - SYE_CLOB1

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Protein

Glutamate--tRNA ligase

Gene
gltX, CLB_1134
Organism
Clostridium botulinum (strain ATCC 19397 / Type A)
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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081Zinc By similarity
Metal bindingi110 – 1101Zinc By similarity
Metal bindingi135 – 1351Zinc By similarity
Metal bindingi137 – 1371Zinc By similarity
Binding sitei255 – 2551ATP By similarity

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

BioCyciCBOT441770:GH1E-1116-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:gltX
Ordered Locus Names:CLB_1134
OrganismiClostridium botulinum (strain ATCC 19397 / Type A)
Taxonomic identifieri441770 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000006379: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Glutamate--tRNA ligaseUniRule annotationPRO_0000330961Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi441770.CLB_1134.

Structurei

3D structure databases

ProteinModelPortaliA7FSY9.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi11 – 2111"HIGH" regionUniRule annotationAdd
BLAST
Motifi252 – 2565"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OMAiIFNYICS.
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.

A7FSY9-1 [UniParc]FASTAAdd to Basket

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MTNKVRTRFA PSPTGYMHVG NLRTALYAYL IAKHDNGDFI LRIEDTDQER    50
LVEGALDVIY NTLKITGLSH DEGPDIGGPV GPYVQSERRN IYIEYAEKLI 100
EKGEAYYCFC SKERLDMLRA NSEALKRPFR YDKHCIDLSK EEIDKKIAEG 150
VPYVIRQKNP TTGSTSFHDE IYGDISVDNS ELDDMILIKS DGLPTYNFAN 200
VVDDHLMGIT HVVRGSEYLS SSPKYNRLYE AFGWDVPIYV HCPPIMKDEH 250
HKLSKRNGDA SFEDLMAKGY LKEAILNYIA LLGWNPGGEK EVFSMEELIE 300
AFNYRNINKA PAVFDTKKLK WMNGEYIRAL SLDKFHEMAL PYYEEALTRD 350
LDTKKISELL HTRVEVLNEI PEQLDFFNNL LEYSPEMYIH KKMKTTYENS 400
LKSLEEVLPK LEALENWTFE NIKEVCMNLV KELEVKNGVV LWPIRTAVSG 450
KQFTPGGAFE IADILGKEET LERIKIGIDK LKALQ 485
Length:485
Mass (Da):55,743
Last modified:September 11, 2007 - v1
Checksum:i4D4264727F64BBB2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000726 Genomic DNA. Translation: ABS34374.1.
RefSeqiYP_001383466.1. NC_009697.1.

Genome annotation databases

EnsemblBacteriaiABS34374; ABS34374; CLB_1134.
GeneIDi5396897.
KEGGicba:CLB_1134.
PATRICi19356862. VBICloBot110701_1066.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000726 Genomic DNA. Translation: ABS34374.1 .
RefSeqi YP_001383466.1. NC_009697.1.

3D structure databases

ProteinModelPortali A7FSY9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 441770.CLB_1134.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS34374 ; ABS34374 ; CLB_1134 .
GeneIDi 5396897.
KEGGi cba:CLB_1134.
PATRICi 19356862. VBICloBot110701_1066.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252720.
KOi K01885.
OMAi IFNYICS.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci CBOT441770:GH1E-1116-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. "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
    Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
    PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19397 / Type A.

Entry informationi

Entry nameiSYE_CLOB1
AccessioniPrimary (citable) accession number: A7FSY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 52 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

Documents

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

External Data

Dasty 3

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