ID SYL_NEIG1 Reviewed; 876 AA. AC Q5FAJ3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 27-MAR-2024, entry version 130. DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; GN OrderedLocusNames=NGO0006; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl- CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA- CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00049}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004969; AAW88778.2; -; Genomic_DNA. DR RefSeq; WP_025456399.1; NC_002946.2. DR RefSeq; YP_207190.2; NC_002946.2. DR PDB; 6YKK; X-ray; 2.24 A; A=1-876. DR PDB; 6YKL; X-ray; 2.27 A; A=1-876. DR PDB; 6YKN; X-ray; 2.63 A; A=1-876. DR PDB; 6YKO; X-ray; 2.21 A; A=1-876. DR PDB; 6YKQ; X-ray; 1.94 A; A=1-876. DR PDB; 6YKS; X-ray; 1.97 A; A=1-876. DR PDB; 6YKT; X-ray; 2.32 A; A=1-876. DR PDB; 6YKU; X-ray; 2.14 A; A=1-876. DR PDB; 6YKV; X-ray; 2.43 A; A=1-876. DR PDB; 6YKW; X-ray; 2.46 A; A=1-876. DR PDB; 6YKX; X-ray; 2.41 A; A=1-876. DR PDB; 7A0P; X-ray; 2.18 A; A=1-876. DR PDB; 7AP2; X-ray; 2.25 A; A=1-876. DR PDBsum; 6YKK; -. DR PDBsum; 6YKL; -. DR PDBsum; 6YKN; -. DR PDBsum; 6YKO; -. DR PDBsum; 6YKQ; -. DR PDBsum; 6YKS; -. DR PDBsum; 6YKT; -. DR PDBsum; 6YKU; -. DR PDBsum; 6YKV; -. DR PDBsum; 6YKW; -. DR PDBsum; 6YKX; -. DR PDBsum; 7A0P; -. DR PDBsum; 7AP2; -. DR AlphaFoldDB; Q5FAJ3; -. DR SMR; Q5FAJ3; -. DR STRING; 242231.NGO_0006; -. DR KEGG; ngo:NGO_0006; -. DR PATRIC; fig|242231.10.peg.7; -. DR HOGENOM; CLU_004427_0_0_4; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1. DR CDD; cd00812; LeuRS_core; 1. DR Gene3D; 2.20.28.290; -; 1. DR Gene3D; 3.10.20.590; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1. DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002302; Leu-tRNA-ligase. DR InterPro; IPR025709; Leu_tRNA-synth_edit. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR NCBIfam; TIGR00396; leuS_bact; 1. DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 2. DR Pfam; PF13603; tRNA-synt_1_2; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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 Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..876 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000334780" FT MOTIF 42..52 FT /note="'HIGH' region" FT MOTIF 634..638 FT /note="'KMSKS' region" FT BINDING 637 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" FT HELIX 7..21 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 22..24 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:6YKV" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:6YKV" FT HELIX 50..68 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 84..93 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 97..114 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 130..145 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 148..159 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 184..193 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 199..204 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 214..224 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 226..236 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 246..249 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 251..257 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 259..264 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 267..270 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 275..281 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 285..296 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 301..304 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 311..319 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 321..323 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 326..332 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 342..346 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 348..350 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 352..361 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 378..380 FT /evidence="ECO:0007829|PDB:6YKL" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 397..399 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 404..417 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 420..427 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:6YKL" FT STRAND 439..441 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 446..449 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 450..452 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 453..456 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 459..461 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 474..476 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 478..481 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 483..486 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 491..493 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 496..499 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 507..510 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 513..516 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 523..527 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 529..535 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 537..544 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 545..547 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 550..564 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 573..580 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 583..591 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:7A0P" FT STRAND 597..600 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 602..604 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 605..607 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 618..620 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 621..623 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 626..634 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 637..640 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 645..652 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 654..664 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 667..669 FT /evidence="ECO:0007829|PDB:6YKV" FT HELIX 675..697 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 714..735 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 740..755 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 762..779 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 780..782 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 784..794 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 799..802 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 809..812 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 820..823 FT /evidence="ECO:0007829|PDB:6YKQ" FT HELIX 841..847 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 865..867 FT /evidence="ECO:0007829|PDB:6YKQ" FT TURN 868..870 FT /evidence="ECO:0007829|PDB:6YKQ" FT STRAND 871..874 FT /evidence="ECO:0007829|PDB:6YKQ" SQ SEQUENCE 876 AA; 98049 MW; E2B73DC55263D03E CRC64; MQEHYQPAAI EPAAQKKWDD ARISNVSEDA SKPKYYCLSM FPYPSGKLHM GHVRNYTIGD VLSRFKLLNG FNVMQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIEYMKT QLKSLGFAID WEREVATCKP EYYRWEQWLF TKLFEKGIVY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG ALIEKREIPM YYFKITDYAE ELLNDLDKLE HWPEQVKTMQ RNWIGKSRGM TVRFAVSDDS KQGLEGDYAK FLQVYTTRPD TLMGATYVAV AAEHPLATAA AADKPELQAF IAECKAGSVA EADMATMEKK GVPTGRYVVN PLNGDKLEVW IANYVLWGYG DGAVMAVPAH DERDFEFAAK YNLPKKQVIA VGDNAFDANR WQEWYGDKEN GVLVNSGDLD GLDFQTAFDA VAAKLQSQGA GEPKTQYRLR DWGISRQRYW GCPIPIVHCE KCGDVPVPAD QLPVVLPENV VPDGMGSPLA KMPEFYETSC PCCGGAAKRE TDTMDTFMES SWYFFRYMSP KFSDGMVSAE SAKYWGAVDQ YIGGIEHAIL HLLYARFFTK LMRDEGLVNV DEPFERLLTQ GMVVCETYYR ENDKGGKDWI NPADVELTFD DKGRPVSAVL KADGLPVVIS GTEKMSKSKN NGVDPQELIN AYGADTARLF MMFAAPPEQS LEWSDSGVEG AHRFLRRLWR TVYEYLKQGG AVKAFAGNQD GLSKELKDLR HKLHSTTAKV SDDYGRRQQF NTAIAAVMEL LNQYDKTDTG SEQGRAVAQE VLEAAVRLLW PIVPHICETL WSELNGAKLW EAGWPTVDEA ALVKSEIEVM VQVNGKLRGK ITVAADASKA DLEAAALANE GAVKFMEGKP AKKIIVVPGR LVNIVV //