ID D3IY83_CAMCO Unreviewed; 199 AA.
AC D3IY83;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 50.
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:ADC39673.1};
OS Campylobacter coli.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195 {ECO:0000313|EMBL:ADC39673.1};
RN [1] {ECO:0000313|EMBL:ADC39673.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cco103 {ECO:0000313|EMBL:ADC39673.1}, and Cco117
RC {ECO:0000313|EMBL:ADC39687.1};
RX PubMed=20097815; DOI=10.1128/AEM.01753-09;
RA Lang P., Lefebure T., Wang W., Pavinski Bitar P., Meinersmann R.J.,
RA Kaya K., Stanhope M.J.;
RT "Expanded multilocus sequence typing and comparative genomic hybridization
RT of Campylobacter coli isolates from multiple hosts.";
RL Appl. Environ. Microbiol. 76:1913-1925(2010).
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};
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DR EMBL; GQ326283; ADC39673.1; -; Genomic_DNA.
DR EMBL; GQ326297; ADC39687.1; -; Genomic_DNA.
DR AlphaFoldDB; D3IY83; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
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:0000313|EMBL:ADC39673.1};
KW Ligase {ECO:0000313|EMBL:ADC39673.1}.
FT DOMAIN 65..196
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:ADC39673.1"
FT NON_TER 199
FT /evidence="ECO:0000313|EMBL:ADC39673.1"
SQ SEQUENCE 199 AA; 23129 MW; F3081A212B6EF9D3 CRC64;
DAFNEAYLSK FKILENLALE EKMKQDALDF NYFDESPTNG ALHPVMSTMD RIIEYFVNLN
FSIEKGPLIE DDFHNFEALN LPKSHPARDM QDTFYFDDKR LLRTQTSPVQ IRTMLAQKPP
IRMIAPGAVF RRDFDITHTP MFHQVEGLVV EEGQKVSFAN LKSILEDFLR YMFGDVKVRF
RPSFFPFTEP SAEVDISCV
//