ARGB_PSEAE
ID ARGB_PSEAE Reviewed; 301 AA.
AC Q9HTN2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082};
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=PA5323;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-18, MASS SPECTROMETRY, AND CRYSTALLIZATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12037312; DOI=10.1107/s0907444902005243;
RA Fernandez-Murga M.L., Ramon-Maiques S., Gil-Ortiz F., Fita I., Rubio V.;
RT "Towards structural understanding of feedback control of arginine
RT biosynthesis: cloning and expression of the gene for the arginine-inhibited
RT N-acetyl-L-glutamate kinase from Pseudomonas aeruginosa, purification and
RT crystallization of the recombinant enzyme and preliminary X-ray studies.";
RL Acta Crystallogr. D 58:1045-1047(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP
RP ANALOG, 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 -!- 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 -!- 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}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:16376937}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}.
CC -!- MASS SPECTROMETRY: Mass=31711; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12037312};
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00082}.
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DR EMBL; AE004091; AAG08708.1; -; Genomic_DNA.
DR PIR; A82980; A82980.
DR RefSeq; NP_254010.1; NC_002516.2.
DR RefSeq; WP_003096572.1; NZ_QZGE01000020.1.
DR PDB; 2BUF; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=2-301.
DR PDBsum; 2BUF; -.
DR AlphaFoldDB; Q9HTN2; -.
DR SMR; Q9HTN2; -.
DR STRING; 287.DR97_2694; -.
DR DrugBank; DB04075; N-Acetyl-L-Glutamate.
DR PaxDb; Q9HTN2; -.
DR PRIDE; Q9HTN2; -.
DR DNASU; 879620; -.
DR EnsemblBacteria; AAG08708; AAG08708; PA5323.
DR GeneID; 879620; -.
DR KEGG; pae:PA5323; -.
DR PATRIC; fig|208964.12.peg.5578; -.
DR PseudoCAP; PA5323; -.
DR HOGENOM; CLU_053680_0_0_6; -.
DR InParanoid; Q9HTN2; -.
DR OMA; EGLYEDW; -.
DR PhylomeDB; Q9HTN2; -.
DR BioCyc; PAER208964:G1FZ6-5445-MON; -.
DR BRENDA; 2.7.2.8; 5087.
DR UniPathway; UPA00068; UER00107.
DR EvolutionaryTrace; Q9HTN2; -.
DR Proteomes; UP000002438; 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; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12037312"
FT CHAIN 2..301
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112650"
FT BINDING 68..69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT ECO:0000269|PubMed:16376937"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082,
FT ECO:0000269|PubMed:16376937"
FT SITE 33
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 255
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT HELIX 5..25
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2BUF"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:2BUF"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:2BUF"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:2BUF"
SQ SEQUENCE 301 AA; 31849 MW; CE0B6E912305B255 CRC64;
MTLSRDDAAQ VAKVLSEALP YIRRFVGKTL VIKYGGNAME SEELKAGFAR DVVLMKAVGI
NPVVVHGGGP QIGDLLKRLS IESHFIDGMR VTDAATMDVV EMVLGGQVNK DIVNLINRHG
GSAIGLTGKD AELIRAKKLT VTRQTPEMTK PEIIDIGHVG EVTGVNVGLL NMLVKGDFIP
VIAPIGVGSN GESYNINADL VAGKVAEALK AEKLMLLTNI AGLMDKQGQV LTGLSTEQVN
ELIADGTIYG GMLPKIRCAL EAVQGGVTSA HIIDGRVPNA VLLEIFTDSG VGTLISNRKR
H
