Reviewed, UniProtKB/Swiss-Prot Q7WKR5 (SYFA_BORBR)

Names and origin

Protein names

Recommended name:
    Phenylalanyl-tRNA synthetase alpha chain
    EC=6.1.1.20
Alternative name(s):
    Phenylalanine--tRNA ligase alpha chain
      Short name=PheRS

Gene names

Name:	pheS
Ordered Locus Names:	BB2040

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00281
Cofactor	Binds 2 magnesium ions per tetramer By similarity.
Subunit structure	Tetramer of two alpha and two beta chains By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00281
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phenylalanyl-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 magnesium ion binding Inferred from electronic annotation. Source: HAMAP phenylalanine-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 – 348	348	Phenylalanyl-tRNA synthetase alpha chain HAMAP MF_00281		PRO_0000126670
Sites
	Metal binding	268	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WKR5-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: F001856A7BA2B5B3	FASTA	348	39,230
	10 20 30 40 50 60 MRFEGSNSMT LLVDDLVSQA QERFAAASDA AALENAKARF LGKEGALTVL LKALGKLDPE 70 80 90 100 110 120 QKREMGARIN QAKQQIEALL NARRAALAQA ELDARLASET IDVTLPGRGK AAGGIHPVIR 130 140 150 160 170 180 TWERVEEIFR SIGFDVADGP EVENDWTNFT ALNNPLDHPA RSMQDTFYVD MHDADGLPLL 190 200 210 220 230 240 LRTHTSPMQV RYARMHKPPI KVIAPGRTYR VDSDATHSPM FHQVEGLWIA EDISFADLKG 250 260 270 280 290 300 VYTDFLRCFF ESDDLVVRFR PSFFPFTEPS AEIDMMFTSG PNRGRWLEIS GSGQVHPQVV 310 320 330 340 RNFGLDPERY IGFAFGSGLE RLTMLRYGVN DLRQFYEGDL RFLRQFNE

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640443 Genomic DNA. Translation: CAE32536.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GenomeReviews	Gene locus BB2040 in contig BX470250_GR.
KEGG	bbr:BB2040.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WKR5.
OMA	FRASYFP.
Enzyme and pathway databases
BioCyc	BBRO257310:BB2040-MON.
BRENDA	6.1.1.20. 413.
Family and domain databases
HAMAP	MF_00281. [Tree]
InterPro	IPR006195. aa-tRNA-synth_II_cons-reg. IPR004529. Phe-tRNA-synth_IIc_asu. IPR004188. Phe-tRNA_synth_II_N. IPR002319. Phenylalanyl-tRNA_Synthase_acu. [Graphical view]
PANTHER	PTHR11538. tRNA-synt_2d. 1 hit.
Pfam	PF02912. Phe_tRNA-synt_N. 1 hit. PF01409. tRNA-synt_2d. 1 hit. [Graphical view]
TIGRFAMs	TIGR00468. pheS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYFA_BORBR

Accession

Primary (citable) accession number: Q7WKR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 39 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)