B7J5K9 (B7J5K9_ACIF2) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 2 HAMAP MF_00022
EC=6.1.1.17 HAMAP MF_00022

Alternative name(s):
Glutamyl-tRNA synthetase 2 HAMAP MF_00022

Gene names

Name:	gltX-1 EMBL ACK78729.1
Synonyms:	gltX2 HAMAP MF_00022
Ordered Locus Names:	AFE_2222

Organism

Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)) [Complete proteome] [HAMAP] EMBL ACK78729.1

Taxonomic identifier

243159 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus

Protein attributes

Sequence length	508 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
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022
Subunit structure	Monomer By similarity. HAMAP MF_00022
Subcellular location	Cytoplasm By similarity HAMAP MF_00022.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. HAMAP MF_00022

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP MF_00022
Cellular component	Cytoplasm HAMAP MF_00022
Ligand	ATP-binding HAMAP MF_00022 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP MF_00022 EMBL ACK78729.1 Ligase
Technical term	Complete 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Motif	42 – 52	11	"HIGH" region By similarity HAMAP MF_00022
	Motif	283 – 287	5	"KMSKS" region By similarity HAMAP MF_00022
Sites
	Binding site	286	1	ATP By similarity HAMAP MF_00022

Sequences

	Sequence		Length	Mass (Da)
	B7J5K9 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 5E42F3613EDF60BE	FASTA	508	55,749
	10 20 30 40 50 60 MSTSQSAFWP ALCEVSYPGF CIAMRPMAQY YTTMNLKSRF APSPTGYLHL GNARTALFAW 70 80 90 100 110 120 LAARGAGGTF ILRLEDTDQQ RSPEIYERAL LEDLRWFGID WDEGPDRGGD HGPYRQMERL 130 140 150 160 170 180 AVYGRYYAHL QSSGQAYACY CSADDLAAER AVQRSAGKAP RYGGRCRHLD AAARAEREAA 190 200 210 220 230 240 GLLPTLRFRV PDQGTLTVPD LVWGERHYAL ADLGDFVIRR SDGSPAFFFA NAVDDALMEV 250 260 270 280 290 300 NLVLRGEDHL TNTPRQILIL QALGLPVPAY GHLPLLLGAD GQPLSKRYGA ASLRDLRKDG 310 320 330 340 350 360 YLAAALRNYL ARLGHHYSAT GFLDSRALAQ GFALNQISRA PSHFDMVQLQ HWQHEAVQSL 370 380 390 400 410 420 DDAAVWNWLA PLLRGKVPMG LEMPFVAAVR ANILLPGDAL DWAERCFGAP ALAADAVEAI 430 440 450 460 470 480 TGVSPEFWSV AQATLQASGG DYRRWTKALQ QASGRRGKAL FMPLRAALTG LTHGPELAAL 490 500 LPLIGEERAL ARLHAAARRP STPIETTL

References

[1]

"Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications." Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II, Eisen J.A., Holmes D.S. BMC Genomics 9:597-597(2008) [PubMed: 19077236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001219 Genomic DNA. Translation: ACK78729.1.
RefSeq	YP_002426620.1. NC_011761.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B7J5K9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7135001.
GenomeReviews	Gene locus AFE_2222 in contig CP001219_GR.
KEGG	afr:AFE_2222.
PATRIC	20655525. VBIAciFer29821_2025.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG628189.
OMA	DQERIEW.
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	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

B7J5K9_ACIF2

Accession

Primary (citable) accession number: B7J5K9

Entry history

Integrated into UniProtKB/TrEMBL:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)