ID SYFB_HAHCH Reviewed; 790 AA. AC Q2SDJ7; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 04-NOV-2026, entry version 105. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283}; DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283}; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283}; DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283}; GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283}; GN OrderedLocusNames=HCH_04574; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Oceanospirillales; Hahellaceae; Hahella. OX NCBI_TaxID=349521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396; RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., RA Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an RT algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(2005). CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Phe) + L-phenylalanine + ATP = L-phenylalanyl-tRNA(Phe) + CC AMP + diphosphate + H(+); 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:0000255|HAMAP-Rule:MF_00283}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00283}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP- CC Rule:MF_00283}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00283}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit CC family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00283}. 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; CP000155; ABC31277.1; -; Genomic_DNA. DR RefSeq; WP_011398342.1; NC_007645.1. DR AlphaFoldDB; Q2SDJ7; -. DR SMR; Q2SDJ7; -. DR STRING; 349521.HCH_04574; -. DR KEGG; hch:HCH_04574; -. DR eggNOG; COG0072; Bacteria. DR eggNOG; COG0073; Bacteria. DR HOGENOM; CLU_016891_0_0_6; -. DR OMA; AACPRYC; -. DR OrthoDB; 9805455at2; -. DR Proteomes; UP000000238; Chromosome. DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IEA:TreeGrafter. 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:InterPro. 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 FunFam; 2.40.50.140:FF:000045; Phenylalanine--tRNA ligase beta subunit; 1. DR FunFam; 3.30.56.10:FF:000002; Phenylalanine--tRNA ligase beta subunit; 1. DR FunFam; 3.30.70.380:FF:000001; Phenylalanine--tRNA ligase beta subunit; 1. DR FunFam; 3.30.930.10:FF:000022; Phenylalanine--tRNA ligase beta subunit; 1. DR FunFam; 3.50.40.10:FF:000001; Phenylalanine--tRNA ligase beta subunit; 1. DR Gene3D; 3.30.56.10; -; 2. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 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 NCBIfam; TIGR00472; pheT_bact; 1. DR NCBIfam; NF045760; YtpR; 1. DR PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1. DR PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 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; SSF54991; Anticodon-binding domain of PheRS; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF56037; PheT/TilS domain; 1. DR SUPFAM; SSF46955; Putative DNA-binding domain; 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..790 FT /note="Phenylalanine--tRNA ligase beta subunit" FT /id="PRO_0000232801" FT DOMAIN 39..147 FT /note="tRNA-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283" FT DOMAIN 400..476 FT /note="B5" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283" FT DOMAIN 696..789 FT /note="FDX-ACB" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283" FT BINDING 454 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283" FT BINDING 460 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283" FT BINDING 463 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283" FT BINDING 464 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283" SQ SEQUENCE 790 AA; 86900 MW; E9BB2827187612F9 CRC64; MKFSEYWLRE WVDPQLSSEA LVQQITMAGL EVDAAERVAK PFSGIVVGEV LSVEPHPDAD KLRVCKVSDG QEEFQVVCGA PNVAAGMKVP FAKIGAVLSG DFKIKKAKLR GVESQGMLCS EEELTLAEKS DGLMPLAADA PVGVDVRSYL KLDDNIIDVD LTPNRSDCLS ILGMAREVAA LNKIPFEAPE VKKTAAVIDD VFPVRVEAPE ACPRYVGRVI KGVDLSAPTP QWMVEKLRRS GIRSIDAVVD VTNFVMIELG QPMHAFDLNE LADGIVVRMP TPGEKLVLLD GQEITINPDT LVIADNEKPL ALAGVMGGEH SGVSEKTKDI FLESAFFAPL HLAGKARSYG LHTDSSHRFE RGVDYAHQAR AIERATELLL EIVGGQPGPV TEICSKEHLP AKALVNLRHA RVDELLGVHL DRTRVEEMLA RLGLGVHKVA KDGWTFSAPT HRFDISIEVD LIEEVARLYG YNKLPVTEPM APLGIKPLPE SKVSLRRLKL HLVSRGYQEA ITYTFVDQKV LSLLTPEEDT ITLANPIASD MAAMRTTLWA GLLQTALYNQ NRQQNRIRLF ESGLRFLKRG GQIQQDPMLA GLIMGASMPE GWESKKRTVD FYDVKGDLES LLEIPGCNLS FRSAQHPALH PGQTAEVLKD GQPIGVLGAL HPRIAKTLNL NGPLYLFELC LNSIADGQVP SFKGVSRFPE IRRDLAIVID EQTPYADVAL AIAQSAGEWR VHHELFDVYH GESVGADKKS LAISIVWRHP ERTLRDEEIT EAFDNVVKEL GNRFGASLRS //