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Acetylglutamate kinase (EC 2.7.2.8) (N-acetyl-L-glutamate 5-phosphotransferase) (NAG kinase) (NAGK)

 ARGB_THEMA              Reviewed;         282 AA.
Q9X2A4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
20-DEC-2017, entry version 135.
RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082};
EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:15342584};
AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082};
AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082};
Short=NAGK {ECO:0000255|HAMAP-Rule:MF_00082};
Name=argB {ECO:0000255|HAMAP-Rule:MF_00082};
OrderedLocusNames=TM_1784;
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
NCBI_TaxID=243274;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
PubMed=10360571; DOI=10.1038/20601;
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Evidence for lateral gene transfer between Archaea and Bacteria from
genome sequence of Thermotoga maritima.";
Nature 399:323-329(1999).
[2]
PROTEIN SEQUENCE OF 1-35, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND MASS SPECTROMETRY.
PubMed=15342584; DOI=10.1128/JB.186.18.6142-6149.2004;
Fernandez-Murga M.L., Gil-Ortiz F., Llacer J.L., Rubio V.;
"Arginine biosynthesis in Thermotoga maritima: characterization of the
arginine-sensitive N-acetyl-L-glutamate kinase.";
J. Bacteriol. 186:6142-6149(2004).
[3]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
ARGININE, MASS SPECTROMETRY, ENZYME REGULATION, AND SUBUNIT.
PubMed=16376937; DOI=10.1016/j.jmb.2005.11.079;
Ramon-Maiques S., Fernandez-Murga M.L., Gil-Ortiz F., Vagin A.,
Fita I., Rubio V.;
"Structural bases of feed-back control of arginine biosynthesis,
revealed by the structures of two hexameric N-acetylglutamate kinases,
from Thermotoga maritima and Pseudomonas aeruginosa.";
J. Mol. Biol. 356:695-713(2006).
-!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-
L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082,
ECO:0000269|PubMed:15342584}.
-!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-
glutamate 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00082,
ECO:0000269|PubMed:15342584}.
-!- ENZYME REGULATION: Allosterically inhibited by arginine.
{ECO:0000269|PubMed:16376937}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Active from 25 to 80 degrees Celsius.
{ECO:0000269|PubMed:15342584};
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
acetyl-L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP-
Rule:MF_00082, ECO:0000269|PubMed:15342584}.
-!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:16376937}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}.
-!- MASS SPECTROMETRY: Mass=30341; Method=MALDI; Range=1-282;
Evidence={ECO:0000269|PubMed:15342584};
-!- MASS SPECTROMETRY: Mass=30352; Method=Electrospray; Range=1-282;
Evidence={ECO:0000269|PubMed:16376937};
-!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
subfamily. {ECO:0000255|HAMAP-Rule:MF_00082}.
-----------------------------------------------------------------------
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EMBL; AE000512; AAD36847.1; -; Genomic_DNA.
PIR; C72211; C72211.
RefSeq; NP_229581.1; NC_000853.1.
RefSeq; WP_004082330.1; NZ_CP011107.1.
PDB; 2BTY; X-ray; 2.75 A; A/B/C=1-282.
PDBsum; 2BTY; -.
ProteinModelPortal; Q9X2A4; -.
SMR; Q9X2A4; -.
STRING; 243274.TM1784; -.
EnsemblBacteria; AAD36847; AAD36847; TM_1784.
GeneID; 897763; -.
KEGG; tma:TM1784; -.
eggNOG; ENOG4105CAS; Bacteria.
eggNOG; COG0548; LUCA.
InParanoid; Q9X2A4; -.
KO; K00930; -.
OMA; PKTECCI; -.
BRENDA; 2.7.2.8; 6331.
UniPathway; UPA00068; UER00107.
EvolutionaryTrace; Q9X2A4; -.
Proteomes; UP000008183; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003991; F:acetylglutamate kinase activity; IBA:GO_Central.
GO; GO:0034618; F:arginine binding; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
Gene3D; 3.40.1160.10; -; 1.
HAMAP; MF_00082; ArgB; 1.
InterPro; IPR036393; AceGlu_kinase-like_sf.
InterPro; IPR004662; AcgluKinase_fam.
InterPro; IPR037528; ArgB.
InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
InterPro; IPR001057; Glu/AcGlu_kinase.
Pfam; PF00696; AA_kinase; 1.
PIRSF; PIRSF000728; NAGK; 1.
PRINTS; PR00474; GLU5KINASE.
SUPFAM; SSF53633; SSF53633; 1.
TIGRFAMs; TIGR00761; argB; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
Arginine biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Kinase; Nucleotide-binding;
Reference proteome; Transferase.
CHAIN 1 282 Acetylglutamate kinase.
/FTId=PRO_0000112678.
REGION 62 63 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00082}.
REGION 266 269 Allosteric inhibitor binding.
BINDING 84 84 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00082}.
BINDING 178 178 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00082,
ECO:0000269|PubMed:16376937}.
BINDING 196 196 Allosteric inhibitor.
BINDING 214 214 Allosteric inhibitor.
SITE 27 27 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_00082}.
SITE 237 237 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_00082}.
HELIX 2 19 {ECO:0000244|PDB:2BTY}.
STRAND 23 28 {ECO:0000244|PDB:2BTY}.
HELIX 31 34 {ECO:0000244|PDB:2BTY}.
HELIX 36 51 {ECO:0000244|PDB:2BTY}.
STRAND 55 60 {ECO:0000244|PDB:2BTY}.
HELIX 64 72 {ECO:0000244|PDB:2BTY}.
STRAND 79 84 {ECO:0000244|PDB:2BTY}.
HELIX 88 100 {ECO:0000244|PDB:2BTY}.
HELIX 102 111 {ECO:0000244|PDB:2BTY}.
TURN 112 114 {ECO:0000244|PDB:2BTY}.
STRAND 117 121 {ECO:0000244|PDB:2BTY}.
HELIX 124 126 {ECO:0000244|PDB:2BTY}.
STRAND 127 132 {ECO:0000244|PDB:2BTY}.
STRAND 140 148 {ECO:0000244|PDB:2BTY}.
HELIX 151 158 {ECO:0000244|PDB:2BTY}.
STRAND 162 170 {ECO:0000244|PDB:2BTY}.
STRAND 172 174 {ECO:0000244|PDB:2BTY}.
STRAND 176 178 {ECO:0000244|PDB:2BTY}.
HELIX 181 192 {ECO:0000244|PDB:2BTY}.
STRAND 195 205 {ECO:0000244|PDB:2BTY}.
HELIX 218 225 {ECO:0000244|PDB:2BTY}.
TURN 226 228 {ECO:0000244|PDB:2BTY}.
HELIX 234 246 {ECO:0000244|PDB:2BTY}.
STRAND 252 256 {ECO:0000244|PDB:2BTY}.
HELIX 262 267 {ECO:0000244|PDB:2BTY}.
STRAND 268 271 {ECO:0000244|PDB:2BTY}.
STRAND 273 277 {ECO:0000244|PDB:2BTY}.
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


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