Reviewed, UniProtKB/Swiss-Prot Q89AU9 (SYI_BUCBP)

Names and origin

Protein names

Recommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS

Gene names

Name:	ileS
Ordered Locus Names:	bbp_139

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	939 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity.
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02002
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	isoleucyl-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 isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 939	939	Isoleucyl-tRNA synthetase HAMAP MF_02002		PRO_0000098366
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP MF_02002
	Motif	603 – 607	5	"KMSKS" region HAMAP MF_02002
Sites
	Metal binding	903	1	Zinc By similarity
	Metal binding	906	1	Zinc By similarity
	Metal binding	922	1	Zinc By similarity
	Metal binding	925	1	Zinc By similarity
	Binding site	562	1	Aminoacyl-adenylate By similarity
	Binding site	606	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89AU9-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: AF3D7233544B22EC	FASTA	939	110,381
	10 20 30 40 50 60 MKDYKTTLNL PKTNFSMKGN LSKKEPFILK KWNDNNIYSL IKKQNIGKKK FFLNDGPPYA 70 80 90 100 110 120 NGNIHIGHAI NKILKDIVIK FKTLSGFDTY YTPSWDCHGL PIEHKVEKTI KKENILITKK 130 140 150 160 170 180 EFRIKCRNYA QSQVNNQKLE FIRLGVFGDW ENSYLTMNFK NEANIARTLM KMFKYGYVYQ 190 200 210 220 230 240 DFKPVHWCIN CKSALAEAEV EYHNKLSNSI IIKFKLAHNI NFWNQIFKND HNQDIHLVVW 250 260 270 280 290 300 TTTPWTLPAS QAIALNPNFK YQLIQTNNNL FIISEKSVPD TMNKMGIQKW KKIHIFLGKN 310 320 330 340 350 360 ISNLKVIHPF LNTTIPVILA DHVTQELGTG IVHTAPEFGQ DDYYACKKNN INFTPTIDKK 370 380 390 400 410 420 GHFLNNIHPK LNNINIFKSI KIVIKLLNNN NALLHSEKLV HSYPYCWRHK TPIISRATQQ 430 440 450 460 470 480 WFININHNNL RNRCIKYIQE VKWIPHWSKN RMIEMIINRP DWCISRQRTW GVPIPIFIHR 490 500 510 520 530 540 KTGKLHPDTI KLSQKIIQNI ETNGIQAWFD ITEKSFLGEL FKQYKKVTDV IDVWFESGSI 550 560 570 580 590 600 QLSNIYNKIQ HQHNNISDLY IEGLDQHRGW FMSSLIISAA ISNQTPYKKV ITHGFVVDKN 610 620 630 640 650 660 KKKMSKSIGN TVHPSEVINT LGSDILRLWT ASTNYSKEMS ISQETLIHIS DYYRRIRNTA 670 680 690 700 710 720 RFLLANLHEF NPENDLINAK NMIILDKWAI GKALHIQKKI IKSYKNYNFH DVIKYLMNFC 730 740 750 760 770 780 SLDMGTFYLE IIKDRQYTTQ KNSIARRSCQ TAMYLILTAF VKWITPILPF TSDELWEYIP 790 800 810 820 830 840 GTNKNKFVFL ELWSNQLFDL NHKDTMNHEY WNQLLIIKTE VNKALEHARQ NKIIRKSLEA 850 860 870 880 890 900 HMTLYVNETI KCNLKLLNKE LKFLFITSKV EIKNFYEAPK DAFQSETITN FKTIIKKMNG 910 920 930 IKCPRCWHII TKIKNNKNHE ICKRCILNTI GPGELRQFL

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26873.1.
RefSeq	NP_777768.1.
3D structure databases
HSSP	HSSP built from PDB template 1FFY based on UniProtKB P41972.
ModBase	Search...
Genome annotation databases
GeneID	1058147.
GenomeReviews	Gene locus bbp_139 in contig AE016826_GR.
KEGG	bab:bbp139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89AU9.
OMA	FPMRGNL.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_139-MON.
Family and domain databases
HAMAP	MF_02002. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR010663. DNA_glyclase/IsotRNA_synth_Znf. IPR002301. Ile-tRNA-synt_Ia. IPR015905. Ile-tRNA-synt_Ia_N. IPR018353. Isoleucyl-tRNA_synthetase. IPR014729. Rossmann-like_a/b/a_fold. IPR013155. V/L/I-tRNA-synth_anticodon-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. PF06827. zf-FPG_IleRS. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_BUCBP

Accession

Primary (citable) accession number: Q89AU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)