ID   LYSZ_PYRCJ              Reviewed;         261 AA.
AC   A3MT40;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Pcal_0372;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000561; ABO07807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MT40; -.
DR   SMR; A3MT40; -.
DR   STRING; 410359.Pcal_0372; -.
DR   EnsemblBacteria; ABO07807; ABO07807; Pcal_0372.
DR   KEGG; pcl:Pcal_0372; -.
DR   eggNOG; arCOG00862; Archaea.
DR   HOGENOM; CLU_053680_2_0_2; -.
DR   OMA; EGLYEDW; -.
DR   UniPathway; UPA00033; UER00036.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000001431; 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; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR037529; LysZ.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   PRINTS; PR00474; GLU5KINASE.
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; Transferase.
FT   CHAIN           1..261
FT                   /note="Putative [LysW]-aminoadipate/[LysW]-glutamate
FT                   kinase"
FT                   /id="PRO_1000010534"
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;  27467 MW;  4AB32B318C9436D2 CRC64;
     MIVVKVGGSV ICKDLSKVVE NLPKYAGEAV VVHGGGCLVN ELLKRMGIEP KFLTHPGGVV
     SRYTDLETLK VFVMAMSWIN KQLVASLFAR GVEAVGLTGA DGGVVRARRK EKVLVVDERG
     RQRVVDGGYV GKIVDVNVKA LAPPPLKVLA PIAVSEKGEL LNVDGDQLAF EVAARAGAGR
     LVILSDVDGL ILGGRVVPRL TPEEAEELAK SEEVRGGMKR KLLMAAEAAR RGVEVVISNG
     LADSPIDAAL GGAGTHISRN I