B0RY28 (SYI_XANCB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoleucine--tRNA ligase
EC=6.1.1.5

Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS

Gene names

Name:	ileS
Ordered Locus Names:	xcc-b100_3183

Organism

Xanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]

Taxonomic identifier

509169 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas campestris › Xanthomonas campestris pv. campestris

Protein attributes

Sequence length	943 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_02002
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule 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. HAMAP-Rule MF_02002
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 regulation of translational fidelity Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: InterPro isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 943	943	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000189216
Regions
	Motif	59 – 69	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	618 – 622	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	906	1	Zinc By similarity
	Metal binding	909	1	Zinc By similarity
	Metal binding	926	1	Zinc By similarity
	Metal binding	929	1	Zinc By similarity
	Binding site	577	1	Aminoacyl-adenylate By similarity
	Binding site	621	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0RY28 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: 5C5D14E3FFEA0CB4	FASTA	943	104,524
	10 20 30 40 50 60 MTQDYKATLH LPATDFPMRG DLPKREPAML ERWEREGLYA QVRANAAGRP LFVLHDGPPY 70 80 90 100 110 120 ANGQIHLGHA VNKILKDIIV KSKYLAGFDA PYIPGWDCHG LPIEIAIEKK FGKVGVKLDA 130 140 150 160 170 180 AQFRQKCREY ATEQIDLQRR DFKRLGVIGD WDNPYKTLDF RFEANEIRAL AKVIDNGHLT 190 200 210 220 230 240 RGVKPVHWCF DCGSALAEAE IEYADKVSPT VDIAYPARDP AAVAAAFGVT LSAGTQVAVP 250 260 270 280 290 300 IWTTTPWTLP ASLAVSLGAE LDYVLVEGAA DHGQPRWLVI AEALAGKALA RYGVDAVVVH 310 320 330 340 350 360 GHAKGAALDQ LLLAHPFYAE RDIPLILGDH VSDDDGTGAV HTAPGHGQED YQVSKQYGLL 370 380 390 400 410 420 ERYSAAQINP IDGRGVYLPS TPPLGDTVLA GLHIWKANDV IIDALRDTGA LLAASKMEHS 430 440 450 460 470 480 YPHCWRHKTP IAFRATPQWF ISMEQANLRA DALKAIETVH WYPSWGQARI AGMIDGRPDW 490 500 510 520 530 540 TISRQRTWGV PIALFVHRET GEPHPRSTEL MRQVAERVEQ GGVDVWYTLD AAELLGDEAG 550 560 570 580 590 600 DYDKITDILD VWFDSGVTHE TVLVDRGLPK PADLYLEGSD QHRGWFQSSL LTGVAMDKVA 610 620 630 640 650 660 PYKQCLTHGF TVDEHGRKMS KSLGNGIEPQ EIMRTLGADI LRLWIASADY SNEMSLSQEI 670 680 690 700 710 720 LKRNADAYRR LRNTARFLLG NLHGFDPLQH LVALDDMVLL DRWIVHRAHE LQEKITAAYA 730 740 750 760 770 780 RYDFAEIVQG LLNFCSVDLG SLYLDVTKDR LYTMAEDARG RRSAQSAMYH VAEAFVRWIA 790 800 810 820 830 840 PVLSFTAEEL WAYLPGEHSG NVLFATWYDG LAPMPADAAL TSADVDKLLA LREQVAKVLE 850 860 870 880 890 900 PMRANGAIGA ALEAEITVAA DAQTAARWQP LSDELRFLFI SGDVTVTAAS TDDIFVSAQP 910 920 930 940 TTKAKCVRCW HHQASVGSDP RHPELCSRCV SNIEGPGEER RWF

References

[1]

"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis." Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A. J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM920689 Genomic DNA. Translation: CAP52548.1.
RefSeq	YP_001904588.1. NC_010688.1.
3D structure databases
ProteinModelPortal	B0RY28.
ModBase	Search...
Protein-protein interaction databases
STRING	509169.xccb100_3183.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAP52548; CAP52548; xcc-b100_3183.
GeneID	6323119.
KEGG	xca:xccb100_3183.
PATRIC	24086268. VBIXanCam108527_3211.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02002. Ile_tRNA_synth_type1.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023585. Ile-tRNA-ligase_type1. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. IPR013155. V/L/I-tRNA-synth_anticodon-bd. IPR009008. Val/Leu/Ile-tRNA-synth_edit. IPR010663. Znf_DNA_glyclase/IsotRNA_synth. [Graphical view]
PANTHER	PTHR11946:SF9. PTHR11946:SF9. 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.
SUPFAM	SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_XANCB

Accession

Primary (citable) accession number: B0RY28

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	April 8, 2008
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program