ARGB_THEMA
ID ARGB_THEMA Reviewed; 282 AA.
AC Q9X2A4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:15342584};
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082};
DE AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE Short=NAGK {ECO:0000255|HAMAP-Rule:MF_00082};
GN Name=argB {ECO:0000255|HAMAP-Rule:MF_00082}; OrderedLocusNames=TM_1784;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-35, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND MASS SPECTROMETRY.
RX PubMed=15342584; DOI=10.1128/jb.186.18.6142-6149.2004;
RA Fernandez-Murga M.L., Gil-Ortiz F., Llacer J.L., Rubio V.;
RT "Arginine biosynthesis in Thermotoga maritima: characterization of the
RT arginine-sensitive N-acetyl-L-glutamate kinase.";
RL J. Bacteriol. 186:6142-6149(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP ARGININE, MASS SPECTROMETRY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=16376937; DOI=10.1016/j.jmb.2005.11.079;
RA Ramon-Maiques S., Fernandez-Murga M.L., Gil-Ortiz F., Vagin A., Fita I.,
RA Rubio V.;
RT "Structural bases of feed-back control of arginine biosynthesis, revealed
RT by the structures of two hexameric N-acetylglutamate kinases, from
RT Thermotoga maritima and Pseudomonas aeruginosa.";
RL J. Mol. Biol. 356:695-713(2006).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC glutamate. {ECO:0000255|HAMAP-Rule:MF_00082,
CC ECO:0000269|PubMed:15342584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00082,
CC ECO:0000269|PubMed:15342584};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by arginine.
CC {ECO:0000269|PubMed:16376937}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Active from 25 to 80 degrees Celsius. {ECO:0000269|PubMed:15342584};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_00082, ECO:0000269|PubMed:15342584}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:16376937}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}.
CC -!- MASS SPECTROMETRY: Mass=30341; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15342584};
CC -!- MASS SPECTROMETRY: Mass=30352; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16376937};
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00082}.
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DR EMBL; AE000512; AAD36847.1; -; Genomic_DNA.
DR PIR; C72211; C72211.
DR RefSeq; NP_229581.1; NC_000853.1.
DR RefSeq; WP_004082330.1; NZ_CP011107.1.
DR PDB; 2BTY; X-ray; 2.75 A; A/B/C=1-282.
DR PDBsum; 2BTY; -.
DR AlphaFoldDB; Q9X2A4; -.
DR SMR; Q9X2A4; -.
DR STRING; 243274.THEMA_05280; -.
DR EnsemblBacteria; AAD36847; AAD36847; TM_1784.
DR KEGG; tma:TM1784; -.
DR eggNOG; COG0548; Bacteria.
DR InParanoid; Q9X2A4; -.
DR OMA; EGLYEDW; -.
DR OrthoDB; 901370at2; -.
DR BRENDA; 2.7.2.8; 6331.
DR UniPathway; UPA00068; UER00107.
DR EvolutionaryTrace; Q9X2A4; -.
DR Proteomes; UP000008183; 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-UniRule.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04250; AAK_NAGK-C; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_00082; ArgB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR037528; ArgB.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR041727; NAGK-C.
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; Allosteric enzyme; Amino-acid biosynthesis;
KW Arginine biosynthesis; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..282
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112678"
FT BINDING 62..63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT ECO:0000269|PubMed:16376937"
FT BINDING 196
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:16376937,
FT ECO:0007744|PDB:2BTY"
FT BINDING 214
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:16376937,
FT ECO:0007744|PDB:2BTY"
FT BINDING 266..269
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:16376937,
FT ECO:0007744|PDB:2BTY"
FT SITE 27
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 237
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 36..51
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:2BTY"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:2BTY"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:2BTY"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2BTY"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:2BTY"
SQ SEQUENCE 282 AA; 30345 MW; A140CE3899BFA40A CRC64;
MRIDTVNVLL EALPYIKEFY GKTFVIKFGG SAMKQENAKK AFIQDIILLK YTGIKPIIVH
GGGPAISQMM KDLGIEPVFK NGHRVTDEKT MEIVEMVLVG KINKEIVMNL NLHGGRAVGI
CGKDSKLIVA EKETKHGDIG YVGKVKKVNP EILHALIEND YIPVIAPVGI GEDGHSYNIN
ADTAAAEIAK SLMAEKLILL TDVDGVLKDG KLISTLTPDE AEELIRDGTV TGGMIPKVEC
AVSAVRGGVG AVHIINGGLE HAILLEIFSR KGIGTMIKEL EG
