SYE_PSEAE
ID SYE_PSEAE Reviewed; 494 AA.
AC Q9XCL6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022};
DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022};
GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=PA3134;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAK;
RX PubMed=10348873; DOI=10.1128/jb.181.11.3582-3586.1999;
RA Franklund C.V., Goldberg J.B.;
RT "Cloning of the glutamyl-tRNA synthetase (gltX) gene from Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 181:3582-3586(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). {ECO:0000255|HAMAP-
CC Rule:MF_00022}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00022};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00022};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00022};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00022}.
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DR EMBL; AF139107; AAD33773.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06522.1; -; Genomic_DNA.
DR PIR; E83254; E83254.
DR RefSeq; NP_251824.1; NC_002516.2.
DR RefSeq; WP_003104596.1; NZ_QZGE01000023.1.
DR PDB; 5TGT; X-ray; 2.45 A; A/B=1-494.
DR PDBsum; 5TGT; -.
DR AlphaFoldDB; Q9XCL6; -.
DR SMR; Q9XCL6; -.
DR STRING; 287.DR97_4795; -.
DR PaxDb; Q9XCL6; -.
DR PRIDE; Q9XCL6; -.
DR EnsemblBacteria; AAG06522; AAG06522; PA3134.
DR GeneID; 882647; -.
DR KEGG; pae:PA3134; -.
DR PATRIC; fig|208964.12.peg.3286; -.
DR PseudoCAP; PA3134; -.
DR HOGENOM; CLU_015768_6_3_6; -.
DR InParanoid; Q9XCL6; -.
DR OMA; WDEGPFF; -.
DR PhylomeDB; Q9XCL6; -.
DR BioCyc; PAER208964:G1FZ6-3194-MON; -.
DR BRENDA; 6.1.1.17; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR033910; GluRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00464; gltX_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..494
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119627"
FT MOTIF 10..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 251..255
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT CONFLICT 93
FT /note="K -> R (in Ref. 1; AAD33773)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5TGT"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:5TGT"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5TGT"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 391..407
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:5TGT"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 451..458
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 460..474
FT /evidence="ECO:0007829|PDB:5TGT"
FT HELIX 479..490
FT /evidence="ECO:0007829|PDB:5TGT"
SQ SEQUENCE 494 AA; 56749 MW; EC3EFD97BA5AFD72 CRC64;
MTTVRTRIAP SPTGDPHVGT AYIALFNLCF ARQHGGQFIL RIEDTDQLRS TRESEQQIYD
ALRWLGIEWD EGPDVGGPHG PYRQSERGHI YKKYSDELVE KGHAFTCFCT PERLDAVRAE
QMARKETPRY DGHCMHLPKD EVQRRLAAGE SHVTRMKVPT EGVCVVPDML RGDVEIPWDR
MDMQVLMKAD GLPTYFLANV VDDHLMGITH VLRGEEWLPS APKLIKLYEY FGWEQPQLCY
MPLLRNPDKS KLSKRKNPTS ITFYERMGYL PQALLNYLGR MGWSMPDERE KFTLAEMIEH
FDLSRVSLGG PIFDLEKLSW LNGQWIREQS VEEFAREVQK WALNPEYLMK IAPHVQGRVE
NFSQIAPLAG FFFSGGVPLD ASLFEHKKLD PTQVRQVLQL VLWKLESLRQ WEKERITGCI
QAVAEHLQLK LRDVMPLMFP AITGHASSVS VLDAMEILGA DLSRYRLRQA LELLGGASKK
ETKEWEKIRD AIPG
