LYSZ_THET2
ID LYSZ_THET2 Reviewed; 269 AA.
AC O50147;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=[LysW]-aminoadipate kinase {ECO:0000255|HAMAP-Rule:MF_02082, ECO:0000305};
DE EC=2.7.2.17 {ECO:0000255|HAMAP-Rule:MF_02082, ECO:0000269|PubMed:25392000};
GN Name=lysZ {ECO:0000255|HAMAP-Rule:MF_02082, ECO:0000303|PubMed:10613839,
GN ECO:0000303|PubMed:19620981}; Synonyms=argB {ECO:0000303|PubMed:9418242};
GN OrderedLocusNames=TT_C1541;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=9418242; DOI=10.1111/j.1574-6968.1997.tb12755.x;
RA Kosuge T., Hoshino T.;
RT "Molecular cloning and sequence analysis of the lysR gene from the
RT extremely thermophilic eubacterium, Thermus thermophilus HB27.";
RL FEMS Microbiol. Lett. 157:73-79(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [3]
RP ROLE IN LYSINE BIOSYNTHESIS, AND PATHWAY.
RX PubMed=10613839; DOI=10.1101/gr.9.12.1175;
RA Nishida H., Nishiyama M., Kobashi N., Kosuge T., Hoshino T., Yamane H.;
RT "A prokaryotic gene cluster involved in synthesis of lysine through the
RT amino adipate pathway: a key to the evolution of amino acid biosynthesis.";
RL Genome Res. 9:1175-1183(1999).
RN [4]
RP ROLE IN LYSINE BIOSYNTHESIS, AND PATHWAY.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=19620981; DOI=10.1038/nchembio.198;
RA Horie A., Tomita T., Saiki A., Kono H., Taka H., Mineki R., Fujimura T.,
RA Nishiyama C., Kuzuyama T., Nishiyama M.;
RT "Discovery of proteinaceous N-modification in lysine biosynthesis of
RT Thermus thermophilus.";
RL Nat. Chem. Biol. 5:673-679(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH ADP AND
RP LYSW-GAMMA-ALPHA-AMINOADIPATE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP MUTAGENESIS OF HIS-57; ARG-111; ARG-112; LYS-113; LYS-117; LYS-123;
RP LYS-125; ARG-128; ARG-227; ARG-230 AND LYS-231.
RX PubMed=25392000; DOI=10.1074/jbc.m114.595983;
RA Yoshida A., Tomita T., Fujimura T., Nishiyama C., Kuzuyama T.,
RA Nishiyama M.;
RT "Structural insight into amino group-carrier protein-mediated lysine
RT biosynthesis: crystal structure of the LysZ.LysW complex from Thermus
RT thermophilus.";
RL J. Biol. Chem. 290:435-447(2015).
CC -!- FUNCTION: Catalyzes the phosphorylation of LysW-gamma-alpha-
CC aminoadipate. Does not phosphorylate N-acetyl-glutamate.
CC {ECO:0000269|PubMed:25392000}.
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 ECO:0000269|PubMed:25392000};
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:0000269|PubMed:10613839,
CC ECO:0000269|PubMed:19620981, ECO:0000305|PubMed:25392000}.
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, ECO:0000305}.
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; AB006681; BAA23879.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS81883.1; -; Genomic_DNA.
DR PIR; T43948; T43948.
DR RefSeq; WP_011173915.1; NC_005835.1.
DR PDB; 3WWM; X-ray; 2.80 A; A=1-269.
DR PDB; 3WWN; X-ray; 1.85 A; A=1-269.
DR PDBsum; 3WWM; -.
DR PDBsum; 3WWN; -.
DR AlphaFoldDB; O50147; -.
DR SMR; O50147; -.
DR STRING; 262724.TT_C1541; -.
DR PRIDE; O50147; -.
DR EnsemblBacteria; AAS81883; AAS81883; TT_C1541.
DR KEGG; tth:TT_C1541; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_053680_2_1_0; -.
DR OMA; EMVYCGK; -.
DR OrthoDB; 901370at2; -.
DR UniPathway; UPA00033; UER00036.
DR Proteomes; UP000000592; 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: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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Lysine biosynthesis; Nucleotide-binding; Transferase.
FT CHAIN 1..269
FT /note="[LysW]-aminoadipate kinase"
FT /id="PRO_0000112712"
FT BINDING 5..8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:25392000,
FT ECO:0007744|PDB:3WWM"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:25392000,
FT ECO:0007744|PDB:3WWM"
FT BINDING 168
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 231
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02082"
FT MUTAGEN 57
FT /note="H->A: Shows reduced activity."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 111
FT /note="R->E: Shows reduced activity."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 112
FT /note="R->E: Shows reduced activity."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 113
FT /note="K->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 117
FT /note="K->E: Does not bind LysW."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 123
FT /note="K->E: Does not bind LysW."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 125
FT /note="K->E: Does not bind LysW."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 128
FT /note="R->E: Does not bind LysW."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 227
FT /note="R->E: Still binds LysW, but shows reduced activity."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 230
FT /note="R->E: Still binds LysW, but shows reduced activity."
FT /evidence="ECO:0000269|PubMed:25392000"
FT MUTAGEN 231
FT /note="K->E: Still binds LysW, but shows reduced activity."
FT /evidence="ECO:0000269|PubMed:25392000"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 171..182
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:3WWN"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:3WWM"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3WWN"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:3WWN"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3WWN"
SQ SEQUENCE 269 AA; 29096 MW; 04F1644B9997CED6 CRC64;
MIVVKVGGAE GINYEAVAKD AASLWKEGVK LLLVHGGSAE TNKVAEALGH PPRFLTHPGG
QVSRLTDRKT LEIFEMVYCG LVNKRLVELL QKEGANAIGL SGLDGRLFVG RRKTAVKYVE
NGKVKVHRGD YTGTVEEVNK ALLDLLLQAG YLPVLTPPAL SYENEAINTD GDQIAALLAT
LYGAEALVYL SNVPGLLARY PDEASLVREI PVERIEDPEY LALAQGRMKR KVMGAVEAVR
GGVKRVVFAD ARVENPIRRA LSGEGTVVR
