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Database: UniProt
Entry: SYFA_SYNPX
LinkDB: SYFA_SYNPX
Original site: SYFA_SYNPX 
ID   SYFA_SYNPX              Reviewed;         335 AA.
AC   Q7TTU6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   18-SEP-2019, entry version 96.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00281};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00281};
GN   Name=pheS {ECO:0000255|HAMAP-Rule:MF_00281};
GN   OrderedLocusNames=SYNW1600;
OS   Synechococcus sp. (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L.,
RA   Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J.,
RA   Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate +
CC         H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413,
CC         Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215;
CC         EC=6.1.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00281};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00281};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00281};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00281}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00281}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00281}.
DR   EMBL; BX569693; CAE08115.1; -; Genomic_DNA.
DR   RefSeq; WP_011128464.1; NC_005070.1.
DR   STRING; 84588.SYNW1600; -.
DR   EnsemblBacteria; CAE08115; CAE08115; SYNW1600.
DR   KEGG; syw:SYNW1600; -.
DR   eggNOG; ENOG4105CSS; Bacteria.
DR   eggNOG; COG0016; LUCA.
DR   HOGENOM; HOG000242675; -.
DR   KO; K01889; -.
DR   OMA; DWHNFTA; -.
DR   OrthoDB; 469058at2; -.
DR   Proteomes; UP000001422; 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:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR   InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    335       Phenylalanine--tRNA ligase alpha subunit.
FT                                /FTId=PRO_0000126781.
FT   METAL       262    262       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00281}.
SQ   SEQUENCE   335 AA;  37178 MW;  50FCA49F49E9B6E9 CRC64;
     MSAPVTLQQL TDQLDALEQQ ATTEISEASD AAALEQLRVG LLGKKGRISG VLWAMGKLPG
     SERPLVGQRA NVLKTQVQSL LAERLAAVKQ AAMAERIARE SIDVTAPASG IPMGHRHPLI
     TTTEEIVDLF LGLGYSVAEG PEVEKDYYNF TALNIPEDHP ARDMQDTFYL QGDLLLRTHT
     SPVQIRHLEQ NPPPVRIVAP GRVYRRDAVD ATHSPVFHQV EVLAIDEGLD FSHLRGTVMA
     FLKAFFGDLP VRFRASYFPF TEPSAEVDVQ WRGRWLEVMG CGMVDPAVLE GLGLDPERYS
     GFAAGLGVER FCMVRHGIDD IRRLYTSDLR FLEQF
//
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