ID   LYSZ_METS5              Reviewed;         262 AA.
AC   A4YD40;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=[LysW]-aminoadipate/[LysW]-glutamate kinase {ECO:0000255|HAMAP-Rule:MF_02082};
DE            EC=2.7.2.- {ECO:0000255|HAMAP-Rule:MF_02082};
DE            EC=2.7.2.17 {ECO:0000255|HAMAP-Rule:MF_02082};
GN   Name=lysZ {ECO:0000255|HAMAP-Rule:MF_02082}; OrderedLocusNames=Msed_0165;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(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         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}.
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DR   EMBL; CP000682; ABP94342.1; -; Genomic_DNA.
DR   RefSeq; WP_011921310.1; NC_009440.1.
DR   AlphaFoldDB; A4YD40; -.
DR   SMR; A4YD40; -.
DR   STRING; 399549.Msed_0165; -.
DR   EnsemblBacteria; ABP94342; ABP94342; Msed_0165.
DR   GeneID; 5104954; -.
DR   GeneID; 59456395; -.
DR   KEGG; mse:Msed_0165; -.
DR   eggNOG; arCOG00862; Archaea.
DR   HOGENOM; CLU_053680_2_0_2; -.
DR   OMA; EGLYEDW; -.
DR   UniPathway; UPA00033; UER00036.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000000242; 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; -; 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   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00761; argB; 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..262
FT                   /note="[LysW]-aminoadipate/[LysW]-glutamate kinase"
FT                   /id="PRO_1000071218"
FT   BINDING         35..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT   BINDING         167
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            224
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
SQ   SEQUENCE   262 AA;  27819 MW;  AFF2BAAB31ADE4B3 CRC64;
     MIVVKIGGRV VKNALQNVIE SVLRYPGKLI LVHGGGDIVS EYTKRMGMEP TFVTSPEGIR
     SRYTSKEELD IYVMTMGLIN KNIVTQLISK GKTAIGITGV DGGSVIGTRK KRIMILDERG
     KKRIIDGGYT GKIVSVNSQL ISSLTSLVDV IVISPIALDT EESTPLNVDG DQMAFNVARA
     VKAEALLLLS DVDGVLLNNA VVKKLSKEEA KELATKIGPG MNRKVLMAAE SVESGVSKVI
     IGSGLVPDAI NSALAGRGTE IS