ID B4R9C7_PHEZH Unreviewed; 807 AA. AC B4R9C7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 103. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283}; DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00283}; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283}; DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00283}; GN Name=pheT {ECO:0000256|HAMAP-Rule:MF_00283, GN ECO:0000313|EMBL:ACG79387.1}; GN OrderedLocusNames=PHZ_c2978 {ECO:0000313|EMBL:ACG79387.1}; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG79387.1, ECO:0000313|Proteomes:UP000001868}; RN [1] {ECO:0000313|EMBL:ACG79387.1, ECO:0000313|Proteomes:UP000001868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG79387.1, RC ECO:0000313|Proteomes:UP000001868}; RX PubMed=18700039; DOI=10.1186/1471-2164-9-386; RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.; RT "Complete genome of Phenylobacterium zucineum - a novel facultative RT intracellular bacterium isolated from human erythroleukemia cell line RT K562."; RL BMC Genomics 9:386-386(2008). 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, ECO:0000256|HAMAP- CC Rule:MF_00283}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00283}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP- CC Rule:MF_00283}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00283}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00283}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit CC family. Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008653, CC ECO:0000256|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; CP000747; ACG79387.1; -; Genomic_DNA. DR RefSeq; WP_012523525.1; NC_011144.1. DR AlphaFoldDB; B4R9C7; -. DR STRING; 450851.PHZ_c2978; -. DR KEGG; pzu:PHZ_c2978; -. DR eggNOG; COG0072; Bacteria. DR eggNOG; COG0073; Bacteria. DR HOGENOM; CLU_016891_0_0_5; -. DR OrthoDB; 9805455at2; -. DR Proteomes; UP000001868; 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-UniRule. 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; 3.30.56.10; -; 2. 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 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 {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00283}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00283}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00283}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00283}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00283}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00283}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00283}; Reference proteome {ECO:0000313|Proteomes:UP000001868}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE- KW ProRule:PRU00209}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE- KW ProRule:PRU00209}. FT DOMAIN 39..148 FT /note="TRNA-binding" FT /evidence="ECO:0000259|PROSITE:PS50886" FT DOMAIN 415..486 FT /note="B5" FT /evidence="ECO:0000259|PROSITE:PS51483" FT DOMAIN 713..806 FT /note="FDX-ACB" FT /evidence="ECO:0000259|PROSITE:PS51447" FT BINDING 464 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283" FT BINDING 470 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283" FT BINDING 473 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283" FT BINDING 474 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283" SQ SEQUENCE 807 AA; 85673 MW; 02CFAD09F98C0B1D CRC64; MKFTLSWLKE HLETDATVEQ VVEAMTMAGL EVESVEDPAA KLAKFTVAKI VEAVQHPNAD KLRVCQVDTK DGRLEIVCGA PNARAGLTTI YAPIGAYVPG SGITLEPRPV RGVVSNGMLC SAKELEVAEE SDGIVELPEA LPVGASAAEA FGLEAVIDFE VTPNRPDWLG VRGIARDLAA AGLGKLKPET VPQVKGSFPC PVEIRVDGTA CPVFGGRLIR GVKNGPSPEW LQKRLASVGL RPINALVDIT NFITHDRARP LHVYDRALMV GDVIEARLGK GPAEPSATDA ASPAAHKDEQ LIALDGKTYD LTPEMSIIAD ADGQRPIGLG GVMGGESTGC SETTTDVFVE CAWFDPIVTA QTGRITGINS DAQYRFARGV DPQSVVPGLE LATAMILELC GGEASEIRLA GEAPAPPAPI AFDRAYVKKL AGLDLPAQRI DAILTDLGFE VAGNAVTPPS WRRDVEGKAD LVEEVARIAG YDNLPTEPLP EVATPAGGVL TLRQRRLRDA RRSLAARGYS EAITWSFMRR AFAELFGGGQ AELVLANPIA SDLDCMRPSA LGNLIEAAAR NARRGFPDAA LFEAGPNFRG DAPGDQWTAV TALVAPHAPK SWTKTAPDPL FALKADLIAL LDELGAPQLQ VVQGQNSPWW HPGRSARLQL GPKVVVAEFG ELHPQVLKAL DAEGPMLAFE VNLDAIPEPK KKGLKTRAAL ELSPLMPLKR DFAFVVSADT PAGDLVRPIL GADKQLIADV RVFDVYQGPG VPEGQKSVAI EVTVQPREKT LTDAEIEALS ARIVAAAEKA AGAKLRG //