LYSZ_SACS2
ID LYSZ_SACS2 Reviewed; 264 AA.
AC Q980X0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=[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, ECO:0000303|PubMed:12042311};
GN Synonyms=argB {ECO:0000303|PubMed:12042311}; OrderedLocusNames=SSO0156;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP INVOLVEMENT IN LYSINE BIOSYNTHESIS.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12042311; DOI=10.1074/jbc.m203528200;
RA Brinkman A.B., Bell S.D., Lebbink R.J., de Vos W.M., van der Oost J.;
RT "The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine
RT biosynthesis in response to lysine availability.";
RL J. Biol. Chem. 277:29537-29549(2002).
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, ECO:0000305|PubMed:12042311}.
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; AE006641; AAK40502.1; -; Genomic_DNA.
DR EMBL; BK000545; DAA00050.1; -; Genomic_DNA.
DR PIR; G90155; G90155.
DR RefSeq; WP_009990381.1; NC_002754.1.
DR AlphaFoldDB; Q980X0; -.
DR SMR; Q980X0; -.
DR STRING; 273057.SSO0156; -.
DR EnsemblBacteria; AAK40502; AAK40502; SSO0156.
DR GeneID; 44129118; -.
DR KEGG; sso:SSO0156; -.
DR PATRIC; fig|273057.12.peg.153; -.
DR eggNOG; arCOG00862; Archaea.
DR HOGENOM; CLU_053680_2_0_2; -.
DR InParanoid; Q980X0; -.
DR OMA; EGLYEDW; -.
DR PhylomeDB; Q980X0; -.
DR UniPathway; UPA00033; UER00036.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IBA:GO_Central.
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:0006526; P:arginine biosynthetic process; IBA:GO_Central.
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..264
FT /note="[LysW]-aminoadipate/[LysW]-glutamate kinase"
FT /id="PRO_0000112704"
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 167
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 224
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
SQ SEQUENCE 264 AA; 28552 MW; D15458B8FEA0AC48 CRC64;
MIVVKIGGRV VKNSLDKIIL DILNINDKVI LVHGGGDIVT DYTKRLGIEP VFVTSPEGIR
SRYTTKEELE VYIMAMSLIN KSITSKLCSL GKNAIGITGV DGGLLLAERK KRIVVIDERG
KKRIIEGGYT GKVKEVRSEI INHLVKLFDI IVVSPIALDV EERTPLNIDG DQAAFAISKA
LRANVLILLS DVEGVLVEGK VINRLTPSEA KELSKKIGPG MNRKLLMAAE SVENGVNKVI
IGSGVKDRPI INALELNGTV IANG
