ID I6DEJ8_SHIBO Unreviewed; 795 AA. AC I6DEJ8; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 11-DEC-2019, entry version 51. 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:EIQ30190.1}; GN ORFNames=SB96558_2311 {ECO:0000313|EMBL:EIQ30190.1}; OS Shigella boydii 965-58. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766138 {ECO:0000313|EMBL:EIQ30190.1, ECO:0000313|Proteomes:UP000004209}; RN [1] {ECO:0000313|EMBL:EIQ30190.1, ECO:0000313|Proteomes:UP000004209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=965-58 {ECO:0000313|EMBL:EIQ30190.1, RC ECO:0000313|Proteomes:UP000004209}; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K., RA Santana-Cruz I., Liu X.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. 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|HAMAP-Rule:MF_00283, CC ECO:0000256|SAAS:SAAS01124689}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-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|HAMAP-Rule:MF_00283, ECO:0000256|SAAS:SAAS01133281}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283, CC ECO:0000256|SAAS:SAAS00710994}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit CC family. Type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00283, CC ECO:0000256|SAAS:SAAS00570605}. 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:EIQ30190.1}. 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; AKNA01000053; EIQ30190.1; -; Genomic_DNA. DR RefSeq; WP_000672365.1; NZ_AKNA01000053.1. DR EnsemblBacteria; EIQ30190; EIQ30190; SB96558_2311. DR PATRIC; fig|766138.3.peg.2360; -. DR Proteomes; UP000004209; Unassembled WGS sequence. 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; 3.30.70.380; -; 1. DR Gene3D; 3.50.40.10; -; 1. DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1. 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; IPR004532; Phe-tRNA-ligase_IIc_bsu. DR InterPro; IPR020825; Phe-tRNA_synthase_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 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 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 {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00461971, ECO:0000313|EMBL:EIQ30190.1}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00461962}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283, ECO:0000256|SAAS:SAAS00710959}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00283, ECO:0000256|SAAS:SAAS00461946, KW ECO:0000313|EMBL:EIQ30190.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00283, ECO:0000256|SAAS:SAAS00244536}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00244576}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00089649}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00462106}; KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209, KW ECO:0000256|SAAS:SAAS00104020}; KW tRNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209, KW ECO:0000256|SAAS:SAAS00469761}. FT DOMAIN 39..148 FT /note="TRNA-binding" FT /evidence="ECO:0000259|PROSITE:PS50886" FT DOMAIN 401..476 FT /note="B5" FT /evidence="ECO:0000259|PROSITE:PS51483" FT DOMAIN 701..794 FT /note="FDX-ACB" FT /evidence="ECO:0000259|PROSITE:PS51447" FT METAL 454 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283" FT METAL 460 FT /note="Magnesium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283" FT METAL 463 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283" FT METAL 464 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283" SQ SEQUENCE 795 AA; 87308 MW; 41BE2F5672D92A69 CRC64; MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFHGVVVGEV VECAQHPNAD KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP GDFKIKAAKL RGEPSEGMLC SFSELGISDD HSGIIELPAD APIGTDIREY LKLDDNTIEI SVTPNRADCL GIIGVARDVA VLNQLPLVEP EIVPVGATID DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR CGIRSIDAVV DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH GLHTDASHRY ERGVDPALQH KAMERATRLL IDICGGEAGP VIDITSEATL PKRATITLRR SKLDRLIGHH IADEQVTDIL RRLGCEVTEG KDEWQAVAPS WRFDMEIEED LVEEVARVYG YNNIPDEPVQ ASLIMGTHRE ADLSLKRVKT LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLPSPISVE MSAMRLSLWT GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR YEEHWNLAKE TVDFYDLKGA LESVLDLTGK LNEVEFRAEA NPALHPGQSA AIYLKGERIG FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI SRFPANRRDI AVVVAENVPA ADILSECKKV GVNQVVGVNL FDVYRGKGVA EGYKSLAISL ILQDTSRTLE EEEIAATVAK CVEALKERFQ ASLRD //