ID LYSX_THET8 Reviewed; 280 AA. AC Q5SH23; Q84BR0; DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Alpha-aminoadipate--LysW ligase LysX; DE Short=AAA--LysW ligase LysX; DE EC=6.3.2.43 {ECO:0000269|PubMed:19620981}; GN Name=lysX; OrderedLocusNames=TTHA1907; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN RP COMPLEX WITH ADP, AND SUBUNIT. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=12963379; DOI=10.1016/s0022-2836(03)00946-x; RA Sakai H., Vassylyeva M.N., Matsuura T., Sekine S., Gotoh K., Nishiyama M., RA Terada T., Shirouzu M., Kuramitsu S., Vassylyev D.G., Yokoyama S.; RT "Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus RT thermophilus HB8."; RL J. Mol. Biol. 332:729-740(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=19620981; DOI=10.1038/nchembio.198; RA Horie A., Tomita T., Saiki A., Kono H., Taka H., Mineki R., Fujimura T., RA Nishiyama C., Kuzuyama T., Nishiyama M.; RT "Discovery of proteinaceous N-modification in lysine biosynthesis of RT Thermus thermophilus."; RL Nat. Chem. Biol. 5:673-679(2009). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATP ANALOG. RX PubMed=23434852; DOI=10.1038/nchembio.1200; RA Ouchi T., Tomita T., Horie A., Yoshida A., Takahashi K., Nishida H., RA Lassak K., Taka H., Mineki R., Fujimura T., Kosono S., Nishiyama C., RA Masui R., Kuramitsu S., Albers S.V., Kuzuyama T., Nishiyama M.; RT "Lysine and arginine biosyntheses mediated by a common carrier protein in RT Sulfolobus."; RL Nat. Chem. Biol. 9:277-283(2013). CC -!- FUNCTION: Catalyzes the ATP-dependent formation of a covalent bond CC between the amino group of alpha-aminoadipate (AAA) and the gamma- CC carboxyl group of the C-terminal glutamate residue in LysW. CC {ECO:0000269|PubMed:19620981}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[amino-group carrier protein]-C-terminal-L-glutamate + ATP + CC L-2-aminoadipate = [amino-group carrier protein]-C-terminal-N-(1,4- CC dicarboxybutan-1-yl)-L-glutamine + ADP + H(+) + phosphate; CC Xref=Rhea:RHEA:41940, Rhea:RHEA-COMP:9693, Rhea:RHEA-COMP:9694, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58672, ChEBI:CHEBI:78503, ChEBI:CHEBI:78525, CC ChEBI:CHEBI:456216; EC=6.3.2.43; CC Evidence={ECO:0000269|PubMed:19620981}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.1 mM for alpha-aminoadipate {ECO:0000269|PubMed:19620981}; CC KM=2.6 mM for ATP {ECO:0000269|PubMed:19620981}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 1/5. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12963379, CC ECO:0000269|PubMed:23434852}. CC -!- SIMILARITY: Belongs to the RimK family. LysX subfamily. {ECO:0000305}. 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; AB103032; BAC67243.1; -; Genomic_DNA. DR EMBL; AP008226; BAD71730.1; -; Genomic_DNA. DR RefSeq; WP_011229004.1; NC_006461.1. DR RefSeq; YP_145173.1; NC_006461.1. DR PDB; 1UC8; X-ray; 2.00 A; A/B=1-280. DR PDB; 1UC9; X-ray; 2.38 A; A/B=1-280. DR PDB; 3VPD; X-ray; 1.95 A; A/B=1-279. DR PDBsum; 1UC8; -. DR PDBsum; 1UC9; -. DR PDBsum; 3VPD; -. DR AlphaFoldDB; Q5SH23; -. DR SMR; Q5SH23; -. DR DIP; DIP-61749N; -. DR EnsemblBacteria; BAD71730; BAD71730; BAD71730. DR GeneID; 3167971; -. DR KEGG; ttj:TTHA1907; -. DR PATRIC; fig|300852.9.peg.1875; -. DR eggNOG; COG0189; Bacteria. DR HOGENOM; CLU_054353_2_1_0; -. DR PhylomeDB; Q5SH23; -. DR BioCyc; MetaCyc:MONOMER-6728; -. DR BRENDA; 6.3.2.43; 2305. DR SABIO-RK; Q5SH23; -. DR UniPathway; UPA00033; UER00035. DR EvolutionaryTrace; Q5SH23; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway. DR GO; GO:0036211; P:protein modification process; IEA:InterPro. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR011870; LysX_arch. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX. DR NCBIfam; TIGR02144; LysX_arch; 1. DR NCBIfam; TIGR00768; rimK_fam; 1. DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1. DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1. DR Pfam; PF08443; RimK; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Ligase; KW Lysine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..280 FT /note="Alpha-aminoadipate--LysW ligase LysX" FT /id="PRO_0000391001" FT DOMAIN 93..276 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT MOTIF 258..259 FT /note="N-[TS] motif that is essential for LysX substrate FT specificity" FT BINDING 89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 133..139 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 169..180 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 202 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 237 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 249 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 249 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 251 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT STRAND 2..8 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 11..22 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 27..31 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 59..71 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 80..87 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 89..99 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 112..122 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 145..158 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 161..164 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 165..170 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 175..184 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 187..195 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 197..200 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 216..228 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 232..241 FT /evidence="ECO:0007829|PDB:3VPD" FT STRAND 244..253 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 259..263 FT /evidence="ECO:0007829|PDB:3VPD" FT HELIX 267..277 FT /evidence="ECO:0007829|PDB:3VPD" SQ SEQUENCE 280 AA; 30718 MW; B168629146AF1344 CRC64; MLAILYDRIR PDERMLFERA EALGLPYKKV YVPALPMVLG ERPKELEGVT VALERCVSQS RGLAAARYLT ALGIPVVNRP EVIEACGDKW ATSVALAKAG LPQPKTALAT DREEALRLME AFGYPVVLKP VIGSWGRLLA KVTDRAAAEA LLEHKEVLGG FQHQLFYIQE YVEKPGRDIR VFVVGERAIA AIYRRSAHWI TNTARGGQAE NCPLTEEVAR LSVKAAEAVG GGVVAVDLFE SERGLLVNEV NHTMEFKNSV HTTGVDIPGE ILKYAWSLAS //