Q9HTN2 (ARGB_PSEAE) Reviewed, UniProtKB/Swiss-Prot

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:	PA5323

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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_B
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP MF_00082_B
Subunit structure	Homohexamer. Ref.3
Subcellular location	Cytoplasm By similarity HAMAP MF_00082_B.
Sequence similarities	Belongs to the acetylglutamate kinase family.
Mass spectrometry	Molecular mass is 31711 Da from positions 2 - 301. Determined by MALDI. Ref.2

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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetylglutamate kinase activity Inferred from electronic annotation. Source: EC glutamate 5-kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 301

300

Acetylglutamate kinase HAMAP MF_00082_B

PRO_0000112650

Regions

Region

68 – 69

2

Substrate binding HAMAP MF_00082_B

Sites

Binding site

90

1

Substrate

Binding site

195

1

Substrate

Site

33

1

Transition state stabilizer

Site

255

1

Transition state stabilizer

Secondary structure

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301

Helix Strand Turn

Details...

Helix

5 – 25

21

Beta strand

29 – 34

6

Turn

37 – 40

4

Helix

43 – 57

15

Beta strand

61 – 66

6

Helix

70 – 78

9

Beta strand

85 – 90

6

Helix

94 – 106

13

Helix

108 – 118

11

Beta strand

123 – 128

6

Helix

130 – 132

3

Beta strand

134 – 138

5

Beta strand

157 – 165

9

Helix

167 – 175

9

Beta strand

179 – 187

9

Beta strand

193 – 195

3

Helix

198 – 209

12

Beta strand

212 – 221

10

Helix

236 – 244

9

Helix

252 – 264

13

Beta strand

268 – 274

7

Helix

280 – 285

6

Beta strand

292 – 296

5

Sequences

	Sequence		Length	Mass (Da)
	Q9HTN2 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CE0B6E912305B255	FASTA	301	31,849
	10 20 30 40 50 60 MTLSRDDAAQ VAKVLSEALP YIRRFVGKTL VIKYGGNAME SEELKAGFAR DVVLMKAVGI 70 80 90 100 110 120 NPVVVHGGGP QIGDLLKRLS IESHFIDGMR VTDAATMDVV EMVLGGQVNK DIVNLINRHG 130 140 150 160 170 180 GSAIGLTGKD AELIRAKKLT VTRQTPEMTK PEIIDIGHVG EVTGVNVGLL NMLVKGDFIP 190 200 210 220 230 240 VIAPIGVGSN GESYNINADL VAGKVAEALK AEKLMLLTNI AGLMDKQGQV LTGLSTEQVN 250 260 270 280 290 300 ELIADGTIYG GMLPKIRCAL EAVQGGVTSA HIIDGRVPNA VLLEIFTDSG VGTLISNRKR H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]	"Towards structural understanding of feedback control of arginine biosynthesis: cloning and expression of the gene for the arginine-inhibited N-acetyl-L-glutamate kinase from Pseudomonas aeruginosa, purification and crystallization of the recombinant enzyme and preliminary X-ray studies." Fernandez-Murga M.L., Ramon-Maiques S., Gil-Ortiz F., Fita I., Rubio V. Acta Crystallogr. D 58:1045-1047(2002) [PubMed: 12037312] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-18, MASS SPECTROMETRY, CRYSTALLIZATION. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]	"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." Ramon-Maiques S., Fernandez-Murga M.L., Gil-Ortiz F., Vagin A., Fita I., Rubio V. J. Mol. Biol. 356:695-713(2006) [PubMed: 16376937] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP ANALOG, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE004091 Genomic DNA. Translation: AAG08708.1.

PIR

A82980.

RefSeq

NP_254010.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BUF	X-ray	2.95	A/B/C/D/E/F/G/H/I/J/K/L	2-301	[»]

ProteinModelPortal

Q9HTN2.

SMR

Q9HTN2. Positions 2-299.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

879620.

GenomeReviews

Gene locus PA5323 in contig AE004091_GR.

KEGG

pae:PA5323.

PATRIC

19845503. VBIPseAer58763_5578.

Organism-specific databases

PseudoCAP

PA5323.

Phylogenomic databases

HOGENOM

HBG497643.

OMA

GGNAMID.

ProtClustDB

PRK00942.

Enzyme and pathway databases

BioCyc

PAER208964:PA5323-MONOMER.

BRENDA

2.7.2.8. 5087.

Family and domain databases

HAMAP

MF_00082_B. ArgB_B.
[Tree]

InterPro

IPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
[Graphical view]

Gene3D

G3DSA:3.40.1160.10. Aa_kinase. 1 hit.

KO

K00930.

Pfam

PF00696. AA_kinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000728. NAGK. 1 hit.

PRINTS

PR00474. GLU5KINASE.

SUPFAM

SSF53633. Aa_kinase. 1 hit.

TIGRFAMs

TIGR00761. ArgB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ARGB_PSEAE

Accession

Primary (citable) accession number: Q9HTN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program