ID LYSZ_IGNH4 Reviewed; 264 AA. AC A8AA51; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Putative [LysW]-aminoadipate/[LysW]-glutamate kinase {ECO:0000255|HAMAP-Rule:MF_02082}; DE EC=2.7.2.17 {ECO:0000255|HAMAP-Rule:MF_02082}; DE EC=2.7.2.19 {ECO:0000255|HAMAP-Rule:MF_02082}; GN Name=lysZ {ECO:0000255|HAMAP-Rule:MF_02082}; GN OrderedLocusNames=Igni_0621; OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Ignicoccus. OX NCBI_TaxID=453591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIN4/I / DSM 18386 / JCM 14125; RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158; RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A., RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C., RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A., RA Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H., RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.; RT "A genomic analysis of the archaeal system Ignicoccus hospitalis- RT Nanoarchaeum equitans."; RL Genome Biol. 9:R158.1-R158.18(2008). CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic CC pathways. Phosphorylates the LysW-bound precursors glutamate (for CC arginine biosynthesis), respectively alpha-aminoadipate (for lysine CC biosynthesis). {ECO:0000255|HAMAP-Rule:MF_02082}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[amino-group carrier protein]-C-terminal-N-(1,4- CC dicarboxybutan-1-yl)-L-glutamine + ATP = [amino-group carrier CC protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L- CC glutamine + ADP; Xref=Rhea:RHEA:41944, Rhea:RHEA-COMP:9694, CC Rhea:RHEA-COMP:9712, ChEBI:CHEBI:30616, ChEBI:CHEBI:78499, CC ChEBI:CHEBI:78503, ChEBI:CHEBI:456216; EC=2.7.2.17; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02082}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[amino-group carrier protein]-C-terminal-gamma-(L-glutamyl)-L- CC glutamate + ATP = [amino-group carrier protein]-C-terminal-gamma-(5- CC phospho-L-glutamyl)-L-glutamate + ADP; Xref=Rhea:RHEA:52632, CC Rhea:RHEA-COMP:13311, Rhea:RHEA-COMP:13313, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:136714, ChEBI:CHEBI:136717, ChEBI:CHEBI:456216; CC EC=2.7.2.19; Evidence={ECO:0000255|HAMAP-Rule:MF_02082}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 2/5. CC {ECO:0000255|HAMAP-Rule:MF_02082}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_02082}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02082}. CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. LysZ CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02082}. 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; CP000816; ABU81803.1; -; Genomic_DNA. DR RefSeq; WP_011998655.1; NC_009776.1. DR AlphaFoldDB; A8AA51; -. DR SMR; A8AA51; -. DR STRING; 453591.Igni_0621; -. DR GeneID; 5563045; -. DR KEGG; iho:Igni_0621; -. DR eggNOG; arCOG00862; Archaea. DR HOGENOM; CLU_053680_2_0_2; -. DR OrthoDB; 6816at2157; -. DR PhylomeDB; A8AA51; -. DR UniPathway; UPA00033; UER00036. DR UniPathway; UPA00068; -. DR Proteomes; UP000000262; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043744; F:N2-acetyl-L-aminoadipate kinase activity; IEA:RHEA. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule. DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1. DR HAMAP; MF_02082; LysZ; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR004662; AcgluKinase_fam. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR037529; LysZ. DR NCBIfam; TIGR00761; argB; 1. DR PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1. DR PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000728; NAGK; 1. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Kinase; Lysine biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..264 FT /note="Putative [LysW]-aminoadipate/[LysW]-glutamate FT kinase" FT /id="PRO_1000010501" FT BINDING 34..35 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082" FT BINDING 61 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082" FT BINDING 169 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082" FT SITE 5 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082" FT SITE 226 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082" SQ SEQUENCE 264 AA; 28079 MW; 22480602AEBA6B23 CRC64; MIVVKAGGRT LLNNMDEIVK SISRLEKAVF VHGGGDLVDE WERKMGMEPQ FKVSASGIKF RYTDEKELEV FVAVLGGLLN KKIVASFASY GRGAVGLTGA DGPSVIAERK KKVIVQEKVG ERLVKRAIAG GYTGKIKEVK TDLIKALVER GLVPVVAPIA LSPEGELLNV NGDQMAAELA KALSAEYLVL LTDVPGVLMD GKVVPEIKSS EAEEVAKKVG PGMNIKIIMA GRVASGGTKV VICDGTVPDP LKCLEERSGT WVVP //