P57230 (SYFB_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenylalanine--tRNA ligase beta chain
EC=6.1.1.20

Alternative name(s):
Phenylalanyl-tRNA synthetase beta chain
Short name=PheRS

Gene names

Name:	pheT
Ordered Locus Names:	BU130

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	795 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00283
Cofactor	Binds 2 magnesium ions per tetramer By similarity. HAMAP MF_00283
Subunit structure	Tetramer of two alpha and two beta chains By similarity.
Subcellular location	Cytoplasm HAMAP MF_00283.
Sequence similarities	Belongs to the phenylalanyl-tRNA synthetase beta chain family. Type 1 subfamily. Contains 1 B5 domain. Contains 1 FDX-ACB domain. Contains 1 tRNA-binding domain.
Caution	Lacks the conserved glutamate residue in position 462 that binds magnesium; it is replaced by a glycine residue.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro tRNA processing Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro phenylalanine-tRNA ligase activity Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 795	795	Phenylalanine--tRNA ligase beta chain HAMAP MF_00283		PRO_0000126856
Regions
	Domain	39 – 148	110	tRNA-binding
	Domain	400 – 475	76	B5
	Domain	701 – 794	94	FDX-ACB
Sites
	Metal binding	453	1	Magnesium By similarity
	Metal binding	459	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	463	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57230 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 46489857F920967A	FASTA	795	91,921
	10 20 30 40 50 60 MKFSEKWLRE WIDPQVSSKI LHEQISNSGI EVEHVENFKS EFHGVVVGKI VQCTFHNESN 70 80 90 100 110 120 NLKVLKVDIG KKKLLNIICG ASNCRNGIKV AVATVGATLP KNITINKKIL KGAWSEGMLC 130 140 150 160 170 180 SFFELGLFLN DNKIIEFPKE TLVGINVYDY FLLEDNIIKV SITSNRPDGL SILGLSRNIA 190 200 210 220 230 240 AINDLRISPL KNRLVPAVIQ KKINIDIQAD KECMNFFGRI IENININVDT PFWMKKKLFF 250 260 270 280 290 300 SNVLSENIIT NIIHYVLIEL GQPLNILDAD NINDSIIVRM ARHEEDLFLK NNIKISLNEN 310 320 330 340 350 360 ILVFSDSNKI LSLPGNINSN IVDVDKNTKN IFLSSYLINR KYISYIIKKM NMNTVLEYHY 370 380 390 400 410 420 YGVDPFLQNY AIEYATDLIL KICGGVPGPI NEKKCNFQIH KNNTIRLHHE RLNKIIGFFI 430 440 450 460 470 480 DTSVISKILY RLDYQLKFQK TFWDVISPSW RFDILIEEDV IGDILRIYEY NNVHLIPLKE 490 500 510 520 530 540 FLNCSKKNEL TDSLLKKSAV ILINQGYHEV INYGFIDPKI QNLIFPNEEN LLLSNPISQD 550 560 570 580 590 600 MSCMRLSLWP GLLKNISYNK NRQQKSIRIF ESGLCFSIDK RENLGIRQEI FLAAAISGNY 610 620 630 640 650 660 IKENWYYNIR KMDFYDLKGD LESILESICQ LNEIEFRRKK IHGLHPEQSA SIYFRNYLIG 670 680 690 700 710 720 SIGAIDPRLE KALNVSSTTF LFEISLNNFS DIKPLKVEEI SKFPTVRRDI AILISEEIAA 730 740 750 760 770 780 YNVIEQCKIF FINEKVEINL FDIYAYKESH NHKKSLGISF IFQNKKRTFQ DNEINLMIDD 790 CIGVLQKKFQ AVLRK

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12848.1.
RefSeq	NP_239962.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57230.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002946; EBBUCP00000002722; EBBUCG00000002946.
GeneID	1109574.
GenomeReviews	Gene locus BU130 in contig BA000003_GR.
KEGG	buc:BU130.
PATRIC	21243774. VBIBucAph127364_0139.
Phylogenomic databases
GeneTree	EBGT00050000007758.
HOGENOM	HBG399638.
OMA	ADKLRVC.
PhylomeDB	P57230.
ProtClustDB	PRK00629.
Enzyme and pathway databases
BioCyc	BSP107806:BU130-MONOMER.
Family and domain databases
HAMAP	MF_00283. Phe_tRNA_synth_beta1. [Tree]
InterPro	IPR005146. B3/B4_tRNA-bd. IPR009061. DNA-bd_dom_put. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004532. Phe-tRNA-synth_IIc_bsu_bac. IPR020825. Phe-tRNA_synthase_B3/B4. IPR005121. PheS_beta_Fdx_antiC-bd. IPR002547. tRNA-bd_dom. IPR005147. tRNA_synthase_B5-dom. [Graphical view]
Gene3D	G3DSA:3.50.40.10. B3_4. 1 hit. G3DSA:3.30.56.20. B5. 1 hit. G3DSA:3.30.70.380. Fdx_AntiC_bd. 1 hit. G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K01890.
Pfam	PF03483. B3_4. 1 hit. PF03484. B5. 1 hit. PF03147. FDX-ACB. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view]
SMART	SM00873. B3_4. 1 hit. SM00874. B5. 1 hit. SM00896. FDX-ACB. 1 hit. [Graphical view]
SUPFAM	SSF56037. B3_4. 1 hit. SSF54991. Fdx_AntiC_bd. 1 hit. SSF50249. Nucleic_acid_OB. 1 hit. SSF46955. Putativ_DNA_bind. 1 hit.
TIGRFAMs	TIGR00472. PheT_bact. 1 hit.
PROSITE	PS51483. B5. 1 hit. PS51447. FDX_ACB. 1 hit. PS50886. TRBD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYFB_BUCAI

Accession

Primary (citable) accession number: P57230

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program