Glutamate--tRNA ligase - Chlorobium tepidum

Contribute

Send feedback

Read comments (?) or add your own

Q9F724 (SYE_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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

Taxonomic identifier

1097 [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 MF_00022_B
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm HAMAP MF_00022_B.
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC
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 MF_00022_B

PRO_0000119541

Regions

Motif

12 – 22

"HIGH" region HAMAP MF_00022_B

Motif

259 – 263

"KMSKS" region HAMAP MF_00022_B

Sites

Binding site

262

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9F724 [UniParc].

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

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: 12093901] [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: 10976061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-503. Strain: ATCC 49652 / DSM 12025 / TLS.
+	Additional computationally mapped references.

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...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1007958.
GenomeReviews	Gene locus CT0299 in contig AE006470_GR.
KEGG	cte:CT0299.
NMPDR	fig\|194439.1.peg.297.
PATRIC	21398713. VBIChlTep116050_0290.
TIGR	CT0299.
Phylogenomic databases
HOGENOM	HBG628189.
OMA	MAHIPLI.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	CTEP194439:CT_0299-MONOMER.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-synth_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]
Gene3D	G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KO	K01885.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 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:	January 25, 2012
This is version 76 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

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents