LYSZ_PYRFU
ID LYSZ_PYRFU Reviewed; 249 AA.
AC Q8U0B5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=PF1684;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL81808.1; -; Genomic_DNA.
DR RefSeq; WP_011012830.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0B5; -.
DR SMR; Q8U0B5; -.
DR STRING; 186497.PF1684; -.
DR PRIDE; Q8U0B5; -.
DR EnsemblBacteria; AAL81808; AAL81808; PF1684.
DR GeneID; 41713515; -.
DR KEGG; pfu:PF1684; -.
DR PATRIC; fig|186497.12.peg.1752; -.
DR eggNOG; arCOG00862; Archaea.
DR HOGENOM; CLU_053680_2_0_2; -.
DR OMA; EGLYEDW; -.
DR OrthoDB; 60029at2157; -.
DR PhylomeDB; Q8U0B5; -.
DR UniPathway; UPA00033; UER00036.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001013; 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..249
FT /note="Putative [LysW]-aminoadipate/[LysW]-glutamate
FT kinase"
FT /id="PRO_0000112701"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT BINDING 166
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 222
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
SQ SEQUENCE 249 AA; 27398 MW; 40D6E69F3D84D270 CRC64;
MRVVKIGGSV ISMLENLWRE NGISEILGNS VIVHGGSRHV DELSRKMGVK IEKLTSPSGV
TFRRTTKEVL KVYVAAMIRA NKEIVEFLRN QGINAIGLTG LDRELIIGER KKLIKAVING
RVVAIRDDYS GVIKKVNTQI LREYLKIGTP VIASIAYDPI ENTPLNVDGD KVAYHVALAM
DAKELYFLSD TAFMAGGKVV SELPADEIEK YLIFAKGGMK KKLLMAKEAI NSGIKNVVIE
GLNGRTVIY
