Glutamate--tRNA ligase - Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)

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Q9F724 (SYE_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	CT0299

Organism

Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]

Taxonomic identifier

194439 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum ›

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Sequence caution	The sequence AAG12192.1 differs from that shown. Reason: Frameshift at position 317.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 503

503

Glutamate--tRNA ligase HAMAP-Rule MF_00022

PRO_0000119541

Regions

Motif

12 – 22

"HIGH" region HAMAP-Rule MF_00022

Motif

259 – 263

"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site

262

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9F724 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 8A265B64E72F4D80
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FASTA

503

57,810

        10         20         30         40         50         60 
MAGQKVRTRF APSPTGYLHV GGLRTALYNY LFAKRMNGDF VIRIEDTDQS RKVEDAEKKL 

        70         80         90        100        110        120 
ISTLEWAGII ADESPMHGGN YGPYVQSQRL SIYRDYCTRL LEDKNAYYCF STPEELEENR 

       130        140        150        160        170        180 
QLQLKQGLQP KYNRKWLPED MGGNMPESEI KKKLDEGAPY VVRMKVPDYV SVWFEDMIRG 

       190        200        210        220        230        240 
PIEFDSATID DQVLMKSDGF PTYHFASVID DHLMEFTHII RGEEWLPSMP KHLLLYEFFG 

       250        260        270        280        290        300 
WEPPKFAHLP LLLNPDRSKL SKRQGDVAVE DYMRKGYSSE AIVNFVALLG WNEGEGSEQE 

       310        320        330        340        350        360 
VFSMEELISK FSLERVGKAG AVFNVEKLSW LEKQYIKTRP VEKIVGNIKP VLQAKLAEFS 

       370        380        390        400        410        420 
PEMSVERITS DDYLAKVVEL MRERVNFEHE FVTFSSYFFF EPESYEEEAV AKRWTPNVPP 

       430        440        450        460        470        480 
LLQEFADLLE ANDDFTAENI EAQLKAFVAP KGLKPAVLIH PIRIAVSGVS FGPSLYHMLE 

       490        500 
VLGKEAVLRR IRRAIERIEV PAA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS.
[2]	"Molecular evidence for the early evolution of photosynthesis." Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E. Science 289:1724-1730(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-503. Strain: ATCC 49652 / DSM 12025 / TLS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006470 Genomic DNA. Translation: AAM71545.1. AF287480 Genomic DNA. Translation: AAG12192.1. Frameshift.
RefSeq	NP_661203.1. NC_002932.3.
3D structure databases
ProteinModelPortal	Q9F724.
ModBase	Search...
Protein-protein interaction databases
STRING	194439.CT0299.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM71545; AAM71545; CT0299.
GeneID	1007958.
KEGG	cte:CT0299.
PATRIC	21398713. VBIChlTep116050_0290.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	RYRDFKG.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	CTEP194439:GHN0-300-MONOMER.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 1.10.8.70. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00022_B. Glu_tRNA_synth_B.
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020752. aa-tRNA-synth_I_codon-bd_sub1. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-ligase_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. 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]
PANTHER	PTHR10119. PTHR10119. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. gltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_CHLTE

Accession

Primary (citable) accession number: Q9F724

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	August 30, 2002
Last modified:	May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents