LYSZ_CALMQ
ID LYSZ_CALMQ Reviewed; 258 AA.
AC A8M8Q8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Cmaq_1300;
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
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., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-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; CP000852; ABW02127.1; -; Genomic_DNA.
DR RefSeq; WP_012186346.1; NC_009954.1.
DR AlphaFoldDB; A8M8Q8; -.
DR SMR; A8M8Q8; -.
DR STRING; 397948.Cmaq_1300; -.
DR EnsemblBacteria; ABW02127; ABW02127; Cmaq_1300.
DR GeneID; 5708965; -.
DR KEGG; cma:Cmaq_1300; -.
DR eggNOG; arCOG00862; Archaea.
DR HOGENOM; CLU_053680_2_0_2; -.
DR OMA; EGLYEDW; -.
DR OrthoDB; 60029at2157; -.
DR UniPathway; UPA00033; UER00036.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001137; 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..258
FT /note="Putative [LysW]-aminoadipate/[LysW]-glutamate
FT kinase"
FT /id="PRO_1000075305"
FT BINDING 33..34
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT BINDING 164
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 258 AA; 27636 MW; 85B94120ED11444B CRC64;
MILVKLGGSV ICGGGLDNVT NDVEPGTVLI HGGGCMVNSV MERMGVKPVI LKHPNGYTSR
YTDEETLKAY VMTMMLINKL IVSKLNARGI RAIGLSGVDL GLVTAKRKER VMIIDERGRT
RVIDGGFSGR VTGVNVNIMN LMLSNSDVVV VSPIALSQEG LMLNVDGDQI AENIAISMNV
KELVILTNVD GVLVNGKPID KVTKANAQEI LQYTTGGMRR KLETALKLTE LGVRTIIANG
LRDKPIRSAL NGLGTVVE
