A4XHE0 (SYE1_CALS8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 1
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1

Gene names

Name:	gltX1
Ordered Locus Names:	Csac_0706

Organism

Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]

Taxonomic identifier

351627 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length	485 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 By similarity HAMAP MF_00022_B.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete 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 – 485	485	Glutamate--tRNA ligase 1 HAMAP MF_00022_B		PRO_0000367631
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP MF_00022_B
	Motif	250 – 254	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	253	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4XHE0 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: 6EA895CBB689A4CE	FASTA	485	56,746
	10 20 30 40 50 60 MEVRTRFAPS PTGHLHIGGA RTALFNYLFA KRYGGKFILR IEDTDLERSS IESEKVIIES 70 80 90 100 110 120 LRWLGIEWDE GVEVGGPYGP YRSTERVDIY KKYVDVLFEK GYAYYCYCTE EELEAQRQEL 130 140 150 160 170 180 LSKGQMPRYL GKCRNLTEDQ KRRFEQEGRK PTVRFKVPEG VKIVVHDLVR GDVEFLSDDI 190 200 210 220 230 240 GDFVIVKSDG IPTYNFAVVI DDHLMKISHV IRGEEHLSNT PRQILIYNAL GFELPQFAHV 250 260 270 280 290 300 SLILGKDRTK MSKRHGSTWV EQYRDQGYLK EGLINFLALL GWSPPEDREI FDMEYLIENF 310 320 330 340 350 360 SLERVSKNPA IFDIDKLNYI NSQHIKLKSL DELTQMCIPY FVEAGYIKED EAKSKFEWLK 370 380 390 400 410 420 KIVKSVYEGL DYLSQIKDRV DIFFNNEVKI EEDEAKEVLK WDHVKDLINV FENKIRQMNE 430 440 450 460 470 480 LTPEAIKLLF KEIQKETGYK GKNLFMPIRV ALTGKTHGPE LVEIIEIVGK ENILKRLEFF KTWYN

References

[1]

"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903." 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., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000679 Genomic DNA. Translation: ABP66325.1.
RefSeq	YP_001179516.1. NC_009437.1.
3D structure databases
ProteinModelPortal	A4XHE0.
ModBase	Search...
Protein-protein interaction databases
STRING	A4XHE0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5087365.
GenomeReviews	Gene locus Csac_0706 in contig CP000679_GR.
KEGG	csc:Csac_0706.
PATRIC	21250976. VBICalSac56748_0811.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	DKETAND.
ProtClustDB	PRK01406.
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	K09698.
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

SYE1_CALS8

Accession

Primary (citable) accession number: A4XHE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	May 29, 2007
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program