SYFB_BUCAI
ID SYFB_BUCAI Reviewed; 795 AA.
AC P57230;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE Short=PheRS;
GN Name=pheT; OrderedLocusNames=BU130;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved glutamate residue in position 462 that
CC binds magnesium; it is replaced by a glycine residue. {ECO:0000305}.
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DR EMBL; BA000003; BAB12848.1; -; Genomic_DNA.
DR RefSeq; NP_239962.1; NC_002528.1.
DR RefSeq; WP_010895964.1; NC_002528.1.
DR AlphaFoldDB; P57230; -.
DR SMR; P57230; -.
DR STRING; 107806.10038813; -.
DR PRIDE; P57230; -.
DR EnsemblBacteria; BAB12848; BAB12848; BAB12848.
DR KEGG; buc:BU130; -.
DR PATRIC; fig|107806.10.peg.139; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_6; -.
DR OMA; ISYNWLK; -.
DR Proteomes; UP000001806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00769; PheRS_beta_core; 1.
DR CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.380; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 1.
DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR033714; tRNA_bind_bactPheRS.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR PANTHER; PTHR10947; PTHR10947; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54991; SSF54991; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00472; pheT_bact; 1.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..795
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126856"
FT DOMAIN 39..148
FT /note="tRNA-binding"
FT DOMAIN 400..475
FT /note="B5"
FT DOMAIN 701..794
FT /note="FDX-ACB"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
SQ SEQUENCE 795 AA; 91921 MW; 46489857F920967A CRC64;
MKFSEKWLRE WIDPQVSSKI LHEQISNSGI EVEHVENFKS EFHGVVVGKI VQCTFHNESN
NLKVLKVDIG KKKLLNIICG ASNCRNGIKV AVATVGATLP KNITINKKIL KGAWSEGMLC
SFFELGLFLN DNKIIEFPKE TLVGINVYDY FLLEDNIIKV SITSNRPDGL SILGLSRNIA
AINDLRISPL KNRLVPAVIQ KKINIDIQAD KECMNFFGRI IENININVDT PFWMKKKLFF
SNVLSENIIT NIIHYVLIEL GQPLNILDAD NINDSIIVRM ARHEEDLFLK NNIKISLNEN
ILVFSDSNKI LSLPGNINSN IVDVDKNTKN IFLSSYLINR KYISYIIKKM NMNTVLEYHY
YGVDPFLQNY AIEYATDLIL KICGGVPGPI NEKKCNFQIH KNNTIRLHHE RLNKIIGFFI
DTSVISKILY RLDYQLKFQK TFWDVISPSW RFDILIEEDV IGDILRIYEY NNVHLIPLKE
FLNCSKKNEL TDSLLKKSAV ILINQGYHEV INYGFIDPKI QNLIFPNEEN LLLSNPISQD
MSCMRLSLWP GLLKNISYNK NRQQKSIRIF ESGLCFSIDK RENLGIRQEI FLAAAISGNY
IKENWYYNIR KMDFYDLKGD LESILESICQ LNEIEFRRKK IHGLHPEQSA SIYFRNYLIG
SIGAIDPRLE KALNVSSTTF LFEISLNNFS DIKPLKVEEI SKFPTVRRDI AILISEEIAA
YNVIEQCKIF FINEKVEINL FDIYAYKESH NHKKSLGISF IFQNKKRTFQ DNEINLMIDD
CIGVLQKKFQ AVLRK
