ID   SYFB_PORPU              Reviewed;         720 AA.
AC   P51346;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit, chloroplastic;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE            Short=PheRS;
GN   Name=pheT;
OS   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 1 subfamily. {ECO:0000305}.
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DR   EMBL; U38804; AAC08232.1; -; Genomic_DNA.
DR   PIR; S73267; S73267.
DR   RefSeq; NP_053956.1; NC_000925.1.
DR   AlphaFoldDB; P51346; -.
DR   SMR; P51346; -.
DR   PRIDE; P51346; -.
DR   GeneID; 810045; -.
DR   GO; GO:0009507; C:chloroplast; 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:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00769; PheRS_beta_core; 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; 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; 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; 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; 2.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Plastid; Protein biosynthesis.
FT   CHAIN           1..720
FT                   /note="Phenylalanine--tRNA ligase beta subunit,
FT                   chloroplastic"
FT                   /id="PRO_0000126995"
FT   DOMAIN          319..404
FT                   /note="B5"
FT   DOMAIN          626..719
FT                   /note="FDX-ACB"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         391
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   720 AA;  82593 MW;  495E49947117F62A CRC64;
     MNFLNKSLIR DSVVLQNRWK IIMKVSLNWL KELAKIEIID AHSLANKLTQ AGFEVEDVEM
     VNIDGHKDYI LDVTSTANRS DVLSMIGLSR EVSALTQADI VKTADIPSAG LFDNISTIIS
     DDSLLNCSYY VSAIMDNIVI QDSPKWLKNR LYSCGFISQN LIIDISNYIM LKWGQPINII
     DLKKIADTNT ESYIEITSNF CSSKQKSVKL DNKDIALSRD VLITQINNNI TSIAGIGINQ
     EFHVDQNTKL IFIEAAIFKE AVVRKSSRSI GIRTESSIRQ ERGLNIDNGR SAYRETLSLL
     IELTHGKVKA TFLKKETENS TLNIDISLKK IQDVLGPIKD NHTVRFLSFD EIENTLKSLQ
     FKITKKDVKK FNVIIPSYRK YDVFREIDIV EEIARVYGYN QFQSKIPKIQ FTKHPSSRRN
     FIDQIRNILR NLGLTELVHY SLVKSKGEIN LKNPLIKDYS TLRSSLLEGL INASAYNIKQ
     SNQTVDGFEI GTVFNLKRNK IIETTKLAII LGGSLDIRSE WSEPAHSLNW YEAKGIIENF
     FRKLNKSIQW VKRESSNDQI NFIQNNKSAT LTYNNDNIGL FGELNELTSS QFGFNTELFV
     LEIDLDILQY SDPEINYLSY RIQPYSKYPC ITRDLCIVIP KKMQINSLFQ LLNQFNDNDL
     ENMTLFDQYS NKLLGNGKKS IGLRFTYRSD HKTLTNLEID NKQNELQKNI IKKLNLEIRK