Reviewed, UniProtKB/Swiss-Prot P41256 (SYY_THIFE)

Names and origin

Protein names

Recommended name:
    Tyrosyl-tRNA synthetase
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS
    TyrRZ

Gene names

Name:	tyrS
Synonyms:	tyrZ

Organism

Thiobacillus ferrooxidans (Acidithiobacillus ferrooxidans)

Taxonomic identifier

920 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). HAMAP MF_02007
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02007
Subunit structure	Homodimer. Ref.2
Subcellular location	Cytoplasm. HAMAP MF_02007
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. Contains 1 S4 RNA-binding domain.
Biophysicochemical properties	Kinetic parameters: KM=0.13 mM for ATP Ref.2 KM=26.8 µM for tyrosine KM=2.54 µM for tRNA(Tyr)

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Gene Ontology (GO)
Biological process	tyrosyl-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 RNA binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-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
Molecule processing
	Chain	1 – 407	407	Tyrosyl-tRNA synthetase HAMAP MF_02007		PRO_0000055666
Regions
	Domain	342 – 403	62	S4 RNA-binding
	Motif	47 – 56	10	"HIGH" region HAMAP MF_02007
	Motif	231 – 235	5	"KMSKS" region HAMAP MF_02007
Sites
	Binding site	234	1	ATP By similarity
Experimental info
	Mutagenesis	53	1	H → A: Does not complement the tyrS mutation in E.coli. Ref.2
	Mutagenesis	306	1	H → A: Does not complement the tyrS mutation in E.coli. 3-fold decrease in Kcat for amino acid activation, without effect on Km for tyrosine or ATP. Ref.2
	Mutagenesis	306	1	H → D: Does not complement the tyrS mutation in E.coli. Ref.2
	Mutagenesis	356	1	S → A: Does not complement the tyrS mutation in E.coli. 7-fold increase in Km for E.coli tRNA, without effect on other kinetic parameters. Ref.2
	Mutagenesis	395	1	K → N: Complements the tyrS mutation in E. coli very poorly. 17-fold increase in Km for E.coli tRNA, without effect on Km for ATP or tyrosine. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P41256-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 7B73FBA2252A2C6B	FASTA	407	45,860
	10 20 30 40 50 60 MTMKHQDAFE QIAFGTVDML PEGEMLARLA AAQRDNRPLR IKLGMDPTAP DLHLGAYVLL 70 80 90 100 110 120 HKARQFQDLG HRLLFVIGDF TAMIGDPTGK SVTRKALSRE EVVANAATYR PQVFKILDPE 130 140 150 160 170 180 RTEVMFNSEW LGALRPEELI QIAACYTVAR MLERDDFNKR YSANQPIAIH EFLYPLLQGY 190 200 210 220 230 240 DSVAIKADVE LGGTDQRFNL LVGRELQREY GQKPQLVLTM PILEGLDGVQ KMSKSLGNFI 250 260 270 280 290 300 AVEDPPAEMF GKIMSISDFL MWRYYALLSR VPAVEQTRLQ KEAASGARNP RDIKLDLAGE 310 320 330 340 350 360 LVRRFHGTAA AQEAHIAFLA RFQRHETPED LPLQAIKLSE APRLSQLLVQ VHLAASTSEA 370 380 390 400 MRKMKEGAVR VDWRRVVDPA TILALDAVYL LQFGKRHFAR VALQKGE

References

[1]	"Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in Escherichia coli." Salazar O., Sagredo B., Jedlicki E., Soell D., Weygand-Durasevic I., Orellana O. J. Bacteriol. 176:4409-4415(1994) [PubMed: 7517395] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Torma.
[2]	"Conserved amino acids near the carboxy terminus of bacterial tyrosyl-tRNA synthetase are involved in tRNA and Tyr-AMP binding." Salazar J.C., Zuniga R., Lefimil C., Soell D., Orellana O. FEBS Lett. 491:257-260(2001) [PubMed: 11240138] [Abstract] Cited for: KINETIC PARAMETERS, MUTAGENESIS OF HIS-53; HIS-306; SER-356 AND LYS-395, SUBUNIT.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X79010 Genomic DNA. Translation: CAA55643.1.
PIR	A55515.
3D structure databases
HSSP	HSSP built from PDB template 1H3E based on UniProtKB P83453.
ModBase	Search...
Enzyme and pathway databases
BRENDA	6.1.1.1. 49.
Family and domain databases
HAMAP	MF_02007. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ib. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA_bd. IPR002307. Tyr-tRNA-synth_Ib_bac/mito. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11766. Tyr_tRNA-synt_1b. 1 hit.
Pfam	PF01479. S4. 1 hit. PF00579. tRNA-synt_1b. 1 hit. [Graphical view]
PRINTS	PR01040. TRNASYNTHTYR.
SMART	SM00363. S4. 1 hit. [Graphical view]
TIGRFAMs	TIGR00234. tyrS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYY_THIFE

Accession

Primary (citable) accession number: P41256

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 59 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)