SYFA_MYCTU
ID SYFA_MYCTU Reviewed; 341 AA.
AC P9WFU3; L0TA22; P94984;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=pheS; OrderedLocusNames=Rv1649; ORFNames=MTCY06H11.14;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 1 subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44414.1; -; Genomic_DNA.
DR PIR; D70620; D70620.
DR RefSeq; NP_216165.3; NC_000962.3.
DR RefSeq; WP_003906646.1; NC_000962.3.
DR PDB; 7DAW; X-ray; 2.83 A; A=1-341.
DR PDB; 7DB7; X-ray; 2.71 A; A=1-341.
DR PDB; 7DB8; X-ray; 2.30 A; A=1-341.
DR PDB; 7K98; X-ray; 2.19 A; A/D=1-341.
DR PDB; 7K9M; X-ray; 2.50 A; A=1-341.
DR PDB; 7KA0; X-ray; 2.40 A; A/D=1-341.
DR PDB; 7KAB; X-ray; 2.50 A; A=1-341.
DR PDBsum; 7DAW; -.
DR PDBsum; 7DB7; -.
DR PDBsum; 7DB8; -.
DR PDBsum; 7K98; -.
DR PDBsum; 7K9M; -.
DR PDBsum; 7KA0; -.
DR PDBsum; 7KAB; -.
DR AlphaFoldDB; P9WFU3; -.
DR SMR; P9WFU3; -.
DR STRING; 83332.Rv1649; -.
DR PaxDb; P9WFU3; -.
DR DNASU; 885105; -.
DR GeneID; 885105; -.
DR KEGG; mtu:Rv1649; -.
DR PATRIC; fig|83332.111.peg.1834; -.
DR TubercuList; Rv1649; -.
DR eggNOG; COG0016; Bacteria.
DR OMA; DWHNFTA; -.
DR PhylomeDB; P9WFU3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; 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; 3.30.930.10; -; 1.
DR HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
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 PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..341
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126733"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000250"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 56..91
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7DB8"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 143..147
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:7KA0"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:7KA0"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:7DB8"
FT STRAND 276..286
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:7K98"
SQ SEQUENCE 341 AA; 37371 MW; C4C31DD8CAEE449B CRC64;
MLSPEALTTA VDAAQQAIAL ADTLDVLARV KTEHLGDRSP LALARQALAV LPKEQRAEAG
KRVNAARNAA QRSYDERLAT LRAERDAAVL VAEGIDVTLP STRVPAGARH PIIMLAEHVA
DTFIAMGWEL AEGPEVETEQ FNFDALNFPA DHPARGEQDT FYIAPEDSRQ LLRTHTSPVQ
IRTLLARELP VYIISIGRTF RTDELDATHT PIFHQVEGLA VDRGLSMAHL RGTLDAFARA
EFGPSARTRI RPHFFPFTEP SAEVDVWFAN KIGGAAWVEW GGCGMVHPNV LRATGIDPDL
YSGFAFGMGL ERTLQFRNGI PDMRDMVEGD VRFSLPFGVG A
