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   27-MAR-2024, entry version 141.
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; Pseudomonadota; 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 /
RC   1C / 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; Evidence={ECO:0000255|HAMAP-
CC         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; 208964.PA3134; -.
DR   PaxDb; 208964-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   OrthoDB; 9807503at2; -.
DR   PhylomeDB; Q9XCL6; -.
DR   BioCyc; PAER208964:G1FZ6-3194-MONOMER; -.
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; HUPs; 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   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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
//