Q5PBW1 (SYE1_ANAMM) 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:	AM039

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	441 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.

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 – 441	441	Glutamate--tRNA ligase 1 HAMAP MF_00022_B		PRO_0000119492
Regions
	Motif	7 – 17	11	"HIGH" region HAMAP MF_00022_B
	Motif	236 – 240	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	239	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PBW1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 3CC9F08ABE6409A6	FASTA	441	50,239
	10 20 30 40 50 60 MITRFAPSPT GYMHIGNART ALICWLYARS RSGKLLLRID DTDLERSENR YVEGIKNDLT 70 80 90 100 110 120 WLAMDWDICF NQRSRISRYD EVFNSLMDAG AVYPCYETPE ELELKRKMML KMGLPPIYDR 130 140 150 160 170 180 SALNMTEQDQ KAYSGRKPYF RLKIGRDQAI SWEDEIRGKV VFQAKNISDP ILRRTDGSYT 190 200 210 220 230 240 YMFPSTVDDI DFEVTHIVRG EDHVSNTAVQ IYIMGLLGAK IPSFAHLPLL RMGGSKMSKR 250 260 270 280 290 300 VGGTEIFKMR DMNLEPMAIN SYMARIGTSL PVEPHTNMRS LVDSFDIKLF NQAPIKFELE 310 320 330 340 350 360 DISKLNVRLL QKLPFAEVQD RLEACGIKCS EGFWYAVRDN INVISEVKGW AEICGPGVTP 370 380 390 400 410 420 VVDDVNRQLL QLASDLLPEG EPNDGTWKTW LQKIKECSGC ETRDILLPLR LALTGVPKGP 430 440 EFAKLLPLIG RVEILRRLRG A

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: St. Maries.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV86218.1.
RefSeq	YP_153473.1. NC_004842.2.
3D structure databases
ProteinModelPortal	Q5PBW1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PBW1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3171397.
GenomeReviews	Gene locus AM039 in contig CP000030_GR.
KEGG	ama:AM039.
PATRIC	20946191. VBIAnaMar46146_0036.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	ARTALIC.
ProtClustDB	PRK12558.
Enzyme and pathway databases
BioCyc	AMAR234826:AM039-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

SYE1_ANAMM

Accession

Primary (citable) accession number: Q5PBW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program