SYFB_DICD3
ID SYFB_DICD3 Reviewed; 795 AA.
AC P37984; E0SDD9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=Dda3937_03678;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 603-795.
RC STRAIN=3937;
RA Douillie A., Toussaint A., Faelen M.;
RL Submitted (AUG-1993) 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 -!- 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}.
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DR EMBL; CP002038; ADM98631.1; -; Genomic_DNA.
DR EMBL; X74749; CAA52767.1; -; Genomic_DNA.
DR PIR; S37139; S37139.
DR RefSeq; WP_013318079.1; NC_014500.1.
DR AlphaFoldDB; P37984; -.
DR SMR; P37984; -.
DR STRING; 198628.Dda3937_03678; -.
DR EnsemblBacteria; ADM98631; ADM98631; Dda3937_03678.
DR GeneID; 9733866; -.
DR KEGG; ddd:Dda3937_03678; -.
DR PATRIC; fig|198628.6.peg.2409; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_6; -.
DR OMA; ISYNWLK; -.
DR OrthoDB; 53568at2; -.
DR BioCyc; DDAD198628:DDA3937_RS11410-MON; -.
DR Proteomes; UP000006859; 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_0000126884"
FT DOMAIN 39..148
FT /note="tRNA-binding"
FT DOMAIN 401..476
FT /note="B5"
FT DOMAIN 701..794
FT /note="FDX-ACB"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 460
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"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT CONFLICT 674
FT /note="D -> A (in Ref. 2; CAA52767)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="R -> A (in Ref. 2; CAA52767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 86564 MW; 38A59E9B8835D130 CRC64;
MKFSELWLRE WVNPAISSDA LSEQITMAGL EVDGVEPVAG AFHGVVVGEV VECAQHPNAD
KLRVTKVNVG GDRLLDIVCG APNCRQGLKV AVATVGAVLP GDFKIKAAKL RGEPSEGMLC
SFSELGISDD HSGIIELPAD APLGTDIREY LKLDDNTIEI SVTPNRADCL GILGVARDVA
VLNELALTAP ATEPVTATIA DRFPIQVDAT EACPRYLGRV VKGINVKAAT PLWMREKLRR
CGIRSIDPVV DVTNYVLLEL GQPMHAFDLN RLEGGIVVRM AKEGETLRLL DGTDATLSAD
TLVIADHQKA LAMGGIFGGE HSGVNGETQD VLLECAYFNP LSITGRARRY GLHTDASHRY
ERGVDPALQH QAMERATRLL LDICGGEAGP VVEAVSEKDL PARATIALRR DKLDRLIGHV
ISDEKVSDIL NRLGCQVTQT ADGWQAVAPS WRFDMAIEED LVEEVARVYG YNNIPNIPTQ
APLKMTQHRE ADLALKRVKT LLVDHGFQEA ITYSFVDPKI QSLIHPGEDA LILPSPISVE
MSAMRLSLWS GLLGAVVHNQ NRQQSRLRLF ESGLRFVPDQ RADLGVRQET MLAGVITGTR
YEEHWDLARQ AVDFYDLKGD LEAVLALTGK LSVLEFRAES HPALHPGQTA AIYLAGERIG
YIGVIHPELE RKLDLNGRTV VFEVLWDKLA ERVVPEAADI SRFPANRRDI AVVVAESVPA
GDVLAECKKV GANQLVGVNL FDVYRGKGVA EGYKSLAISL VLQDTARTLA EEEIAATVAQ
CVAALKQRFQ ASLRD
