Reviewed, UniProtKB/Swiss-Prot P0A6C8 (ARGB_ECOLI)

Names and origin

Protein names

Recommended name:
    Acetylglutamate kinase
    EC=2.7.2.8
Alternative name(s):
    NAG kinase
      Short name=AGK
    N-acetyl-L-glutamate 5-phosphotransferase

Gene names

Name:	argB
Ordered Locus Names:	b3959, JW5553

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP MF_00082
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP MF_00082
Subunit structure	Homodimer. Ref.7
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the acetylglutamate kinase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP acetylglutamate kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 258

258

Acetylglutamate kinase HAMAP MF_00082

PRO_0000112614

Regions

Nucleotide binding

181 – 186

6

ATP HAMAP MF_00082

Nucleotide binding

209 – 211

3

ATP HAMAP MF_00082

Region

44 – 45

2

Substrate binding HAMAP MF_00082

Sites

Binding site

66

1

Substrate HAMAP MF_00082

Binding site

158

1

Substrate HAMAP MF_00082

Site

8

1

Transition state stabilizer HAMAP MF_00082

Site

217

1

Transition state stabilizer HAMAP MF_00082

Experimental info

Mutagenesis

8

1

K → R: Reduces activity 50-fold. Increases KM for N-acetyl-L-glutamate and ATP about 10-fold. Ref.5

Mutagenesis

66

1

R → K: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP nearly 20-fold. Ref.5

Mutagenesis

158

1

N → Q: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP over 20-fold. Ref.5

Mutagenesis

162

1

D → E: Reduces activity over 99%. No effect on KM for N-acetyl-L-glutamate and ATP. Ref.5

Secondary structure

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258

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

11 – 15

5

Helix

17 – 31

15

Beta strand

38 – 42

5

Helix

45 – 55

11

Helix

70 – 81

12

Helix

83 – 94

12

Beta strand

99 – 102

4

Helix

106 – 108

3

Beta strand

110 – 114

5

Helix

117 – 119

3

Beta strand

120 – 127

8

Helix

131 – 138

8

Beta strand

142 – 145

4

Beta strand

147 – 150

4

Beta strand

156 – 158

3

Helix

161 – 172

12

Beta strand

175 – 184

10

Helix

198 – 206

9

Helix

213 – 228

16

Beta strand

232 – 238

7

Helix

240 – 242

3

Helix

243 – 247

5

Beta strand

252 – 256

5

Sequences

	Sequence		Length	Mass (Da)
	P0A6C8-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 8B916B8CBC143738	FASTA	258	27,160
	10 20 30 40 50 60 MMNPLIIKLG GVLLDSEEAL ERLFSALVNY RESHQRPLVI VHGGGCVVDE LMKGLNLPVK 70 80 90 100 110 120 KKNGLRVTPA DQIDIITGAL AGTANKTLLA WAKKHQIAAV GLFLGDGDSV KVTQLDEELG 130 140 150 160 170 180 HVGLAQPGSP KLINSLLENG YLPVVSSIGV TDEGQLMNVN ADQAATALAA TLGADLILLS 190 200 210 220 230 240 DVSGILDGKG QRIAEMTAAK AEQLIEQGII TDGMIVKVNA ALDAARTLGR PVDIASWRHA 250 EQLPALFNGM PMGTRILA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes." Parsot C., Boyen A., Cohen G.N., Glansdorff N. Gene 68:275-283(1988) [PubMed: 2851495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase." Marco-Marin C., Ramon-Maiques S., Tavarez S., Rubio V. J. Mol. Biol. 334:459-476(2003) [PubMed: 14623187] [Abstract] Cited for: MUTAGENESIS OF LYS-8; ARG-66; ASN-158 AND ASP-162.
[6]	"N-acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms." Gil F., Ramon-Maiques S., Marina A., Fita I., Rubio V. Acta Crystallogr. D 55:1350-1352(1999) [PubMed: 10393305] [Abstract] Cited for: CRYSTALLIZATION.
[7]	"Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis." Ramon-Maiques S., Marina A., Gil-Ortiz F., Fita I., Rubio V. Structure 10:329-342(2002) [PubMed: 12005432] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP ANALOG, SUBUNIT.
[8]	"The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic." Gil-Ortiz F., Ramon-Maiques S., Fita I., Rubio V. J. Mol. Biol. 331:231-244(2003) [PubMed: 12875848] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ATP AND TRANSITION STATE ANALOG.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M21446 Genomic DNA. Translation: AAA23478.1.
U00006 Genomic DNA. Translation: AAC43065.1.
U00096 Genomic DNA. Translation: AAC76941.3.
AP009048 Genomic DNA. Translation: BAE77352.1. Different initiation.

PIR

KIECAE. JT0331.

RefSeq

AP_003851.1.
NP_418394.3.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GS5	X-ray	1.50	A	1-258	[»]
1GSJ	X-ray	1.85	A	1-258	[»]
1OH9	X-ray	1.91	A	1-258	[»]
1OHA	X-ray	1.90	A	1-258	[»]
1OHB	X-ray	1.90	A	1-258	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6C8. 2 interactions.

Genome annotation databases

GeneID

948464.

GenomeReviews

Gene locus JW5553 in contig AP009048_GR.
Gene locus b3959 in contig U00096_GR.

KEGG

ecj:JW5553.
eco:b3959.

Organism-specific databases

EchoBASE

EB0062.

EcoGene

EG10064. argB.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6C8.

OMA

P0A6C8. MVLCGST.

Enzyme and pathway databases

BioCyc

EcoCyc:ACETYLGLUTKIN-MON.
MetaCyc:ACETYLGLUTKIN-MON.

Family and domain databases

HAMAP

MF_00082.
[Tree]

InterPro

IPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR011148. GlcNAc_kinase.
[Graphical view]

Gene3D

G3DSA:3.40.1160.10. Aa_kinase. 1 hit.

Pfam

PF00696. AA_kinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000728. NAGK. 1 hit.

TIGRFAMs

TIGR00761. argB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ARGB_ECOLI

Accession

Primary (citable) accession number: P0A6C8
Secondary accession number(s): P11445, Q2M8Q4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)