ID E9LHG2_9LACO Unreviewed; 111 AA. AC E9LHG2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 24-JUL-2024, entry version 44. DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814}; DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814}; DE Flags: Fragment; GN Name=pheS {ECO:0000313|EMBL:ADW23136.1}; OS Liquorilactobacillus vini. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Liquorilactobacillus. OX NCBI_TaxID=238015 {ECO:0000313|EMBL:ADW23136.1}; RN [1] {ECO:0000313|EMBL:ADW23136.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TR7.5.7 {ECO:0000313|EMBL:ADW23136.1}; RX PubMed=21092306; DOI=10.1186/1471-2180-10-298; RA Lucena B.T., Dos Santos B.M., Moreira J.L., Moreira A.P., Nunes A.C., RA Azevedo V., Miyoshi A., Thompson F.L., de Morais M.A.; RT "Diversity of lactic acid bacteria of the bioethanol process."; RL BMC Microbiol. 10:298-298(2010). RN [2] {ECO:0000313|EMBL:ADW23136.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TR7.5.7 {ECO:0000313|EMBL:ADW23136.1}; RA de Lucena B.T.L., dos Santos B.M., Moreira J.L.S., Moreira A.P.B., RA Nunes A.C., Azevedo V.A., Thompson F.L., de Morais M.A.Jr.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; CC Evidence={ECO:0000256|ARBA:ARBA00000395}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HQ009778; ADW23136.1; -; Genomic_DNA. DR AlphaFoldDB; E9LHG2; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0016740; F:transferase activity; IEA:UniProt. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:TreeGrafter. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 4: Predicted; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000313|EMBL:ADW23136.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}. FT DOMAIN 12..88 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ADW23136.1" FT NON_TER 111 FT /evidence="ECO:0000313|EMBL:ADW23136.1" SQ SEQUENCE 111 AA; 12449 MW; 0F0F3840543CD85E CRC64; TNLEKHDFSQ GPLKMISPGK VYRRDTDDAT HSHQFHQVEG LVIDKHVTMA DLKGTLEKIA QTVFGAKRQI RLRPSYFPFT EPSVEVDVSC FKCGGKGCQV CKQTGWIEVL G //