Q8NQN7 (SYFA_CORGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	pheS
Ordered Locus Names:	Cgl1389, cg1574

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. HAMAP MF_00281
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.
Sequence caution	The sequence CAF21400.1 differs from that shown. Reason: Erroneous initiation.

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 Reference proteome
Gene Ontology (GO)
Biological process	phenylalanyl-tRNA aminoacylation 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phenylalanine-tRNA ligase activity Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 340	340	Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281		PRO_0000126696
Sites
	Metal binding	258	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NQN7 [UniParc]. Last modified October 19, 2002. Version 1. Checksum: 082BBECB5079AC60	FASTA	340	37,846
	10 20 30 40 50 60 MTEASLNEAA DAAIKAFDGA QNLDELAALR RDHLGDAAPI PQARRSLGTI PKDQRKDAGR 70 80 90 100 110 120 FVNMALGRAE KHFAQVKVVL EEKRNAEVLE LERVDVTVPT TREQVGALHP ITILNEQIAD 130 140 150 160 170 180 IFVGMGWEIA EGPEVEAEYF NFDALNFLPD HPARTLQDTF HIAPEGSRQV LRTHTSPVQV 190 200 210 220 230 240 RTMLNREVPI YIACPGRVFR TDELDATHTP VFHQIEGLAV DKGLTMAHLR GTLDHLAKEL 250 260 270 280 290 300 FGPETKTRMR SNYFPFTEPS AEVDVWFPNK KGGAGWIEWG GCGMVNPNVL RAVGVDPEEY 310 320 330 340 TGFAFGMGIE RTLQFRNGLS DMRDMVEGDI RFTLPFGIQA

References

[1]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB98782.1. BX927152 Genomic DNA. Translation: CAF21400.1. Different initiation.
RefSeq	NP_600608.1. NC_003450.3. YP_225676.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NQN7.
ModBase	Search...
2D gel databases
World-2DPAGE	0001:Q8NQN7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1019365. 3342992.
GenomeReviews	Gene locus Cgl1389 in contig BA000036_GR. Gene locus cg1574 in contig BX927147_GR.
KEGG	cgb:cg1574. cgl:NCgl1335.
PATRIC	21494815. VBICorGlu203724_1357.
Phylogenomic databases
HOGENOM	HBG284353.
OMA	FRASYFP.
PhylomeDB	Q8NQN7.
ProtClustDB	PRK00488.
Enzyme and pathway databases
BioCyc	CGLU196627:CG1574-MONOMER.
Family and domain databases
HAMAP	MF_00281. Phe_tRNA_synth_alpha1. [Tree]
InterPro	IPR006195. aa-tRNA-synth_II. IPR004529. Phe-tRNA-synth_IIc_asu. IPR004188. Phe-tRNA_synth_II_N. IPR022911. Phe_tRNA_synth_alpha1_bac. IPR002319. Phenylalanyl-tRNA_Synthase. IPR010978. tRNA-bd_arm. [Graphical view]
KO	K01889.
Pfam	PF02912. Phe_tRNA-synt_N. 1 hit. PF01409. tRNA-synt_2d. 1 hit. [Graphical view]
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMs	TIGR00468. PheS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYFA_CORGL

Accession

Primary (citable) accession number: Q8NQN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 19, 2002
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program