Q5NQQ7 (SYI_ZYMMO) 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:	ZMO0323

Organism

Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]

Taxonomic identifier

264203 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas › Zymomonas mobilis › Zymomonas mobilis subsp. mobilis

Protein attributes

Sequence length	941 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 – 941	941	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_0000098513
Regions
	Motif	69 – 79	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	630 – 634	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	915	1	Zinc By similarity
	Metal binding	918	1	Zinc By similarity
	Metal binding	932	1	Zinc By similarity
	Metal binding	935	1	Zinc By similarity
	Binding site	589	1	Aminoacyl-adenylate By similarity
	Binding site	633	1	ATP By similarity
Experimental info
	Sequence conflict	92 – 94	3	SQT → TKP in AAD56932. Ref.1
	Sequence conflict	140	1	E → K in AAD56932. Ref.1
	Sequence conflict	181	1	A → S in AAD56932. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5NQQ7 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 645DF7E9C0E82279	FASTA	941	106,263
	10 20 30 40 50 60 MSDQKSADAT QARDWRPTVF LPKTSFPMKA GLAKKEPEIL ARWQKEDLYQ QLREQRKGAE 70 80 90 100 110 120 RFILHDGPPY ANGDIHIGHA LNKILKDIIM RSQTLLGKDV PYIPGWDCHG LPIEWKVEEQ 130 140 150 160 170 180 FRKKKLNVDK DVNAVEFRQE CRKYAVHWVD TQRQEFKRLG VLGEWDNPYL TMNFEAEAII 190 200 210 220 230 240 AGELMRFSET GQIYRGAKPV LWSVVEKTAL AEAEVDYADV DSTTIDLAFK ITDSKIPELV 250 260 270 280 290 300 GGYAVIWTTT PWTIPANRAL AYGPDIDYVL VDLNGKHYLF AEALLEDSLK RIGHEGDAPV 310 320 330 340 350 360 LWRGKGAELD GSIAQHPMFE KGGFFAEPRP FLGGSHVTTE AGTGIVHMAP DYGEDDFLLC 370 380 390 400 410 420 KAHNIDPVFA VEDDGRYRKD WLWMGGEGLV ISPKINAADG PICSDLREVG ALLATSVLHH 430 440 450 460 470 480 SYPHSWRSKA KLIYRCTPQW FIALDRPVEK GAIAGKTLRE TALKAIDEVS WFPAKGKNRI 490 500 510 520 530 540 QTMVEGRPDW VISRQRAWGV PITLYVNRES GDYLRDPEVN ARILAAFRKE GADAWFKANH 550 560 570 580 590 600 QLFLGDKYRL EDYEPVNDIL DVWFDSGSTH AFVVEARYGE GTRAQLYLEG SDQHRGWFQS 610 620 630 640 650 660 SLLESCGSRG HAPYEAVLTH GFTLDGTGRK MSKSVGNVID PLKVINESGA DILRMWVAST 670 680 690 700 710 720 DYNEDVRISK EVLSGTSDGY RKLRNSFRYL LGALEGFSEE EKVDLADLPE LEKYILHLLA 730 740 750 760 770 780 ELDQALHESV NGFAFNRYLR LLSDFVNNDL SAFFFDIRKD RLYCDVGEAA PQGTEERRAY 790 800 810 820 830 840 RTVLDILFHA LVRYAAPILC FTAEEVWLHR FPDAGSVHLS VWPEVDGQWK NAVLGEKWAV 850 860 870 880 890 900 IREQRQIVTE KIEPLRREKI VGSSLEAEVT LPVDAATAKI LSSVDFSEIC ITAKINLVDA 910 920 930 940 SDAAITVDRT QNHKCGRCWQ HLPEVEEDGA LCDRCKSVVG E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Lee H.J., Kang H.S. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.
[2]	"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4." Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. , Kang H.L., Lee S.Y., Lee K.J., Kang H.S. Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF180145 Genomic DNA. Translation: AAD56932.1. AE008692 Genomic DNA. Translation: AAV88947.1.
RefSeq	YP_162058.1. NC_006526.2.
3D structure databases
ProteinModelPortal	Q5NQQ7.
ModBase	Search...
Protein-protein interaction databases
STRING	264203.ZMO0323.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAV88947; AAV88947; ZMO0323.
GeneID	3188160.
KEGG	zmo:ZMO0323.
PATRIC	32565986. VBIZymMob102260_0307.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
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. [Graphical view]
PANTHER	PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 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_ZYMMO

Accession

Primary (citable) accession number: Q5NQQ7
Secondary accession number(s): Q9RNJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	February 1, 2005
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program