LYSZ_PYRHO
ID LYSZ_PYRHO Reviewed; 249 AA.
AC O59398;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=PH1718;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30832.1; -; Genomic_DNA.
DR PIR; A71180; A71180.
DR AlphaFoldDB; O59398; -.
DR SMR; O59398; -.
DR STRING; 70601.3258149; -.
DR EnsemblBacteria; BAA30832; BAA30832; BAA30832.
DR KEGG; pho:PH1718; -.
DR eggNOG; arCOG00862; Archaea.
DR UniPathway; UPA00033; UER00036.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000000752; 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; Transferase.
FT CHAIN 1..249
FT /note="Putative [LysW]-aminoadipate/[LysW]-glutamate
FT kinase"
FT /id="PRO_0000112702"
FT BINDING 64
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 10
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; 27847 MW; 6C1209090EFC8305 CRC64;
MRWVSMRVIK VGGSVLENLE KVFKPEIFRD AVVVHGGSRY VDELAKKLGL NVEKLTSPSG
VTFRRTTRKV LDVYIAAVMK ANRELVSFLR RQGIEAIGVS GVKEVIIGRR KKLIKAVING
KIMAIRDDYS GIIKEVNVEM IRNYMKVGVP VIAPIAYDPV ENVPLNVDGD KVAYHVALAL
KSRELYFLSD TAFLINGEVI DKIPRNRIEE YFPYSSGGMR KKLLMAKKAI ESGVERVIIE
GLNGRTVIS
