SYFM_ARATH
ID SYFM_ARATH Reviewed; 429 AA.
AC Q94K73; Q9M2K2;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Phenylalanine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.20 {ECO:0000305};
DE AltName: Full=Phenylalanyl-tRNA synthetase {ECO:0000305};
DE Short=PheRS {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At3g58140; ORFNames=F9D24.50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=17433818; DOI=10.1016/j.jmb.2007.03.015;
RA Pujol C., Marechal-Drouard L., Duchene A.M.;
RT "How can organellar protein N-terminal sequences be dual targeting signals?
RT In silico analysis and mutagenesis approach.";
RL J. Mol. Biol. 369:356-367(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-54, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Is responsible for the charging of tRNA(Phe) with
CC phenylalanine in mitochondrial translation. {ECO:0000250}.
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:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:16251277, ECO:0000269|PubMed:17433818,
CC ECO:0000269|PubMed:18431481}. Mitochondrion matrix
CC {ECO:0000269|PubMed:16251277, ECO:0000269|PubMed:17433818,
CC ECO:0000269|PubMed:18431481}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AL137081; CAB68152.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79747.1; -; Genomic_DNA.
DR EMBL; AF370247; AAK44062.1; -; mRNA.
DR EMBL; AY063063; AAL34237.1; -; mRNA.
DR PIR; T45974; T45974.
DR RefSeq; NP_567061.1; NM_115676.2.
DR AlphaFoldDB; Q94K73; -.
DR SMR; Q94K73; -.
DR BioGRID; 10298; 1.
DR STRING; 3702.AT3G58140.1; -.
DR iPTMnet; Q94K73; -.
DR PaxDb; Q94K73; -.
DR PRIDE; Q94K73; -.
DR ProteomicsDB; 228479; -.
DR EnsemblPlants; AT3G58140.1; AT3G58140.1; AT3G58140.
DR GeneID; 824983; -.
DR Gramene; AT3G58140.1; AT3G58140.1; AT3G58140.
DR KEGG; ath:AT3G58140; -.
DR Araport; AT3G58140; -.
DR TAIR; locus:2085455; AT3G58140.
DR eggNOG; KOG2783; Eukaryota.
DR HOGENOM; CLU_022696_1_0_1; -.
DR InParanoid; Q94K73; -.
DR OMA; SKSDTYY; -.
DR OrthoDB; 1115196at2759; -.
DR PhylomeDB; Q94K73; -.
DR PRO; PR:Q94K73; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94K73; baseline and differential.
DR Genevisible; Q94K73; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 3.30.70.380; -; 1.
DR Gene3D; 3.30.930.10; -; 2.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; SSF54991; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00469; pheS_mito; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase;
KW Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 54..429
FT /note="Phenylalanine--tRNA ligase,
FT chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000390362"
FT DOMAIN 338..429
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00778"
FT BINDING 163..166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192..194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199..201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 429 AA; 49252 MW; A90E9A18D070C47F CRC64;
MTVFSVQSTI FSRASVALLS SNGFKRFSFV SSFSSSAAYS PPKMRKRRYP IVSAVDIGGV
AIARNDVVRE DDPTNNVPDS IFSKLGMQLH RRDKHPIGIL KNAIYDYFDS NYSNKFEKFE
DLSPIVTTKQ NFDDVLVPAD HVSRSLNDTY YVDSQTVLRC HTSAHQAELL RKGHSRFLVT
GDVYRRDSID STHYPVFHQM EGFCVFSPED WNGSGKDSTL YAAEDLKKCL EGLARHLFGS
VEMRWVDTYF PFTNPSFELE IYFKEDWLEV LGCGVTEQVI LKQSGLENNV AWAFGLGLER
LAMVLFDIPD IRFFWSSDER FTSQFGKGEL GVKFKPYSKY PPCYKDISFW ISDLFTENNF
CEVVRGIAGD LVEEVKLIDQ FTNKKKGLTS HCYRIVFRSM ERSLTDEEVN DLQSKVRDEV
QKKLNVELR
