ID   LYSZ_CENSY              Reviewed;         266 AA.
AC   A0RWW1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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}; OrderedLocusNames=CENSYa_1204;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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; DP000238; ABK77828.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RWW1; -.
DR   SMR; A0RWW1; -.
DR   STRING; 414004.CENSYa_1204; -.
DR   EnsemblBacteria; ABK77828; ABK77828; CENSYa_1204.
DR   KEGG; csy:CENSYa_1204; -.
DR   PATRIC; fig|414004.10.peg.1096; -.
DR   HOGENOM; CLU_053680_2_0_2; -.
DR   OMA; EGLYEDW; -.
DR   UniPathway; UPA00033; UER00036.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000000758; 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..266
FT                   /note="Putative [LysW]-aminoadipate/[LysW]-glutamate
FT                   kinase"
FT                   /id="PRO_1000075307"
FT   BINDING         36..37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT   BINDING         168
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            225
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
SQ   SEQUENCE   266 AA;  28180 MW;  C99836F07C39E443 CRC64;
     MITIKIGGSI VDSLHPSAIP DIKKAAAGGV VLVHGGGKEV TKVCEQLGKE PRFVTSPGNI
     KSRYTDKETA EIFTMVMSGR INKCIVRMLQ QHGVNAVGLS GIDGGLIRAE RKSRLVIVNE
     RGRKQAIEGG YTGRITSVNS ELLETLLGKG IVPVVSPIAM GNEYELLNVD GDRAAANIAG
     ATKSERILFV TDVDGLMMDE KLVSRLSAAE AEEIRPKIGP GMEKKVLAAT EALKMGVREA
     IIARGSRENP VSAAIAHENC TVIGDG