Reviewed, UniProtKB/Swiss-Prot P94282 (SYFA_BORBU)

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:	BB_0513

Organism

Borrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	528 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_00282
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_00282
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 2 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 – 528	528	Phenylalanyl-tRNA synthetase alpha chain HAMAP MF_00282		PRO_0000126804
Experimental info
	Sequence conflict	146	1	T → S in AAB41018. Ref.2
	Sequence conflict	407 – 418	12	IVIED…SIKTL → LLLRMVLALKLC Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P94282-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: C5C97D529BBD6D07	FASTA	528	59,952
	10 20 30 40 50 60 MKVIFMKADL NLIKTLHPLE IKVIVNNEEE DDISASIIIE KLGFNEGQAN KTIEWLNSKG 70 80 90 100 110 120 IIEEIYRKLN VFYKATERGL GALRDGFVEE KIINLVSQKA VLASNLALEL DIDVKEVRKA 130 140 150 160 170 180 FGNLLKEGIL SLDLDKQIII NCLDGTETNY QKVRVLLERA KNSDLLRESL TTEELLLISN 190 200 210 220 230 240 FAKKKGADSV FFKIIEKLDL KFRLSSFGLE VKNFLMKSKL TGDELTKLTP EILKNKTYEN 250 260 270 280 290 300 KKFRAYNIHI PSAKTFIGRA NSYLDYISKI KDKLVGLGFQ EFDGPLVETE FFNNDALFMP 310 320 330 340 350 360 QFHPSRDIKD VYYISDPSMQ ESLPEPYFSN VKLAHETGYA TGSRGWRYSF SEDLSKRLVL 370 380 390 400 410 420 RTHGTVLSAK QLINAKNPSR YFGVIRCFRY DQVDATHGVD FYQTEGIVIE DGVSIKTLLG 430 440 450 460 470 480 LLEIFAKELA GATEIKYVPA YFPFTEPSIE IHVKHPVLGW FELGGSGIFR PEVTKPLGID 490 500 510 520 LPVIAWGIGI DRMALMHLGL NDLRDLFTYD IGDVILRRGK IDAKVRNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]	"Phenylalanyl-tRNA synthetase genes (alpha and beta subunits) and thioredoxin reductase gene of Borrelia burgdorferi." Barbour A.G., Hinnebusch J. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-418. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000783 Genomic DNA. Translation: AAC66871.1. U82978 Genomic DNA. Translation: AAB41018.1.
PIR	H70163.
RefSeq	NP_212647.1.
3D structure databases
HSSP	HSSP built from PDB template 1JJC based on UniProtKB P27001.
ModBase	Search...
Genome annotation databases
GeneID	1195359.
GenomeReviews	Gene locus BB_0513 in contig AE000783_GR.
KEGG	bbu:BB0513.
NMPDR	fig|224326.1.peg.897.
TIGR	BB_0513.
Phylogenomic databases
HOGENOM	P94282.
OMA	IGIDRMA.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0513-MON.
BRENDA	6.1.1.20. 142596.
Family and domain databases
HAMAP	MF_00282. [Tree]
InterPro	IPR006195. aa-tRNA-synth_II_cons-reg. IPR004529. Phe-tRNA-synth_IIc_asu. IPR002319. Phenylalanyl-tRNA_Synthase_acu. [Graphical view]
PANTHER	PTHR11538. tRNA-synt_2d. 1 hit.
Pfam	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_BORBU

Accession

Primary (citable) accession number: P94282
Secondary accession number(s): O51466

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 30, 2000
Last modified:	November 3, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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