ID W4V2Q7_9FIRM Unreviewed; 243 AA.
AC W4V2Q7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=JCM21531_336 {ECO:0000313|EMBL:GAE86999.1};
OS Acetivibrio straminisolvens JCM 21531.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE86999.1, ECO:0000313|Proteomes:UP000019109};
RN [1] {ECO:0000313|EMBL:GAE86999.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE86999.1};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT Isolated from a Cellulose-Degrading Bacterial Community.";
RL Genome Announc. 2:e00110-14(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAE86999.1}.
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DR EMBL; BAVR01000003; GAE86999.1; -; Genomic_DNA.
DR AlphaFoldDB; W4V2Q7; -.
DR STRING; 1294263.JCM21531_336; -.
DR Proteomes; UP000019109; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR NCBIfam; TIGR00468; pheS; 1.
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:GAE86999.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:GAE86999.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019109}.
FT DOMAIN 21..221
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 243 AA; 27413 MW; 2B4DEE3781A51752 CRC64;
MPGKRKMLGK KHPLSIVIDE IKDVFIGMGY EIAEGPEIEL DYYNFEALNI PKNHPARDVQ
DTFYINNNIL LRTQTSPVQI RVMENKKPPI KIICPGRVYR SDAVDATHSP IFHQVEGLVV
DKGITMGDLV GTLRLFAKSL FGEKTEIRLR PHHFPFTEPS AEVDVSCWAC GGTGCRVCKN
EGWIEILGAG MVHPKVLEIC GIDPEVYSGF AFGLGVERTA MGRFNIDDMR LLYENDIRFL
KQF
//