Acetylglutamate kinase - Escherichia coli (strain K12)

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P0A6C8 (ARGB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetylglutamate kinase
EC=2.7.2.8

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

Gene names

Name:	argB
Ordered Locus Names:	b3959, JW5553

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP-Rule MF_00082_B
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP-Rule MF_00082_B
Subunit structure	Homodimer. Ref.7
Subcellular location	Cytoplasm Probable HAMAP-Rule MF_00082_B.
Sequence similarities	Belongs to the acetylglutamate kinase family.
Sequence caution	The sequence BAE77352.1 differs from that shown. Reason: Erroneous initiation.

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 Reference proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from direct assay PubMed 17651682. Source: EcoCyc response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki
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 direct assay Ref.6. Source: EcoCyc
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-Rule MF_00082_B

PRO_0000112614

Regions

Nucleotide binding

181 – 186

ATP HAMAP-Rule MF_00082_B

Nucleotide binding

209 – 211

ATP HAMAP-Rule MF_00082_B

Region

44 – 45

Substrate binding HAMAP-Rule MF_00082_B

Sites

Binding site

Substrate

Binding site

158

Substrate

Site

Transition state stabilizer

Site

217

Transition state stabilizer

Experimental info

Mutagenesis

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

Mutagenesis

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

Mutagenesis

158

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

Mutagenesis

162

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

Secondary structure

258

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6C8 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 8B916B8CBC143738
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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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ATP AND TRANSITION STATE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_418394.3. NC_000913.2.
YP_491493.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
2WXB	X-ray	2.00	A/B	1-258	[»]
2X2W	X-ray	2.00	A/B	1-258	[»]

ProteinModelPortal

P0A6C8.

SMR

P0A6C8. Positions 1-258.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6C8. 2 interactions.

MINT

MINT-1309378.

STRING

511145.b3959.

Proteomic databases

PaxDb

P0A6C8.

PRIDE

P0A6C8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76941; AAC76941; b3959.
BAE77352; BAE77352; BAE77352.

GeneID

12932895.
948464.

KEGG

ecj:Y75_p3229.
eco:b3959.

PATRIC

32123439. VBIEscCol129921_4080.

Organism-specific databases

EchoBASE

EB0062.

EcoGene

EG10064. argB.

Phylogenomic databases

eggNOG

COG0548.

HOGENOM

HOG000233260.

K00930.

OMA

GGCLVDD.

ProtClustDB

PRK00942.

Enzyme and pathway databases

BioCyc

EcoCyc:ACETYLGLUTKIN-MONOMER.
ECOL316407:JW5553-MONOMER.
MetaCyc:ACETYLGLUTKIN-MONOMER.

SABIO-RK

P0A6C8.

UniPathway

UPA00068; UER00107.

Gene expression databases

Genevestigator

P0A6C8.

Family and domain databases

Gene3D

3.40.1160.10. 1 hit.

HAMAP

MF_00082_B. ArgB_B.

InterPro

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

Pfam

PF00696. AA_kinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000728. NAGK. 1 hit.

SUPFAM

SSF53633. Aa_kinase. 1 hit.

TIGRFAMs

TIGR00761. argB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6C8.

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:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents