ID   LYSZ_PYRAE              Reviewed;         261 AA.
AC   Q8ZU99;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Putative [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}; Synonyms=argB;
GN   OrderedLocusNames=PAE2882;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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}.
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; AE009441; AAL64509.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZU99; -.
DR   SMR; Q8ZU99; -.
DR   STRING; 178306.PAE2882; -.
DR   PRIDE; Q8ZU99; -.
DR   EnsemblBacteria; AAL64509; AAL64509; PAE2882.
DR   KEGG; pai:PAE2882; -.
DR   PATRIC; fig|178306.9.peg.2154; -.
DR   eggNOG; arCOG00862; Archaea.
DR   HOGENOM; CLU_053680_2_0_2; -.
DR   InParanoid; Q8ZU99; -.
DR   OMA; EGLYEDW; -.
DR   UniPathway; UPA00033; UER00036.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IBA:GO_Central.
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:0006526; P:arginine biosynthetic process; IBA:GO_Central.
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..261
FT                   /note="Putative [LysW]-aminoadipate/[LysW]-glutamate
FT                   kinase"
FT                   /id="PRO_0000112700"
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         162
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            221
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
SQ   SEQUENCE   261 AA;  27934 MW;  B66F7A72526ABC85 CRC64;
     MIVVKIGGSV VCKDASKVIQ NLPKYADRAV VIHGGGCLVN ELLKRMGIEP KFLTHPGGLV
     SRYTDWETLK VFVMAMGWIN KYIVASLHGL GVQALGLTGA DLGVVVAKRK ERVLVIDERG
     RQRVVDGGYV GKIAEIRVDK LTPPPLKVLA PVAVSEKGEL LNIDGDQLAF DVAREAKAER
     LILLSDVEGL ILGGKVVPRL TPEEAEKLVK SEEVRGGMKR KLLMASEAAK LGIEVVISSG
     LVDSPIDAAL NGAGTHIIKN I