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Protein

Acetylglutamate kinase

Gene

argB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.UniRule annotation

Catalytic activityi

ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.UniRule annotation

Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Arginine biosynthesis bifunctional protein ArgJ (argJ), Amino-acid acetyltransferase (argA)
  2. Acetylglutamate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. Succinylornithine transaminase/acetylornithine aminotransferase (aruC)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei33Transition state stabilizerUniRule annotation1
Binding sitei90SubstrateUniRule annotation1 Publication1
Binding sitei195SubstrateUniRule annotation1 Publication1
Sitei255Transition state stabilizerUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processAmino-acid biosynthesis, Arginine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.2.8. 5087.
UniPathwayiUPA00068; UER00107.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylglutamate kinaseUniRule annotation (EC:2.7.2.8UniRule annotation)
Alternative name(s):
N-acetyl-L-glutamate 5-phosphotransferaseUniRule annotation
NAG kinaseUniRule annotation
Short name:
NAGKUniRule annotation
Gene namesi
Name:argBUniRule annotation
Ordered Locus Names:PA5323
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5323.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB04075. N-Acetyl-L-Glutamate.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001126502 – 301Acetylglutamate kinaseAdd BLAST300

Proteomic databases

PaxDbiQ9HTN2.
PRIDEiQ9HTN2.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5323.

Structurei

Secondary structure

1301
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 25Combined sources21
Beta strandi29 – 34Combined sources6
Turni37 – 40Combined sources4
Helixi43 – 57Combined sources15
Beta strandi61 – 66Combined sources6
Helixi70 – 78Combined sources9
Beta strandi85 – 90Combined sources6
Helixi94 – 106Combined sources13
Helixi108 – 118Combined sources11
Beta strandi123 – 128Combined sources6
Helixi130 – 132Combined sources3
Beta strandi134 – 138Combined sources5
Beta strandi157 – 165Combined sources9
Helixi167 – 175Combined sources9
Beta strandi179 – 187Combined sources9
Beta strandi193 – 195Combined sources3
Helixi198 – 209Combined sources12
Beta strandi212 – 221Combined sources10
Helixi236 – 244Combined sources9
Helixi252 – 264Combined sources13
Beta strandi268 – 274Combined sources7
Helixi280 – 285Combined sources6
Beta strandi292 – 296Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BUFX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L2-301[»]
ProteinModelPortaliQ9HTN2.
SMRiQ9HTN2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HTN2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni68 – 69Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the acetylglutamate kinase family. ArgB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAS. Bacteria.
COG0548. LUCA.
HOGENOMiHOG000233259.
InParanoidiQ9HTN2.
KOiK00930.
OMAiPKTECCI.
PhylomeDBiQ9HTN2.

Family and domain databases

HAMAPiMF_00082. ArgB. 1 hit.
InterProiView protein in InterPro
IPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
PfamiView protein in Pfam
PF00696. AA_kinase. 1 hit.
PIRSFiPIRSF000728. NAGK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9HTN2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLSRDDAAQ VAKVLSEALP YIRRFVGKTL VIKYGGNAME SEELKAGFAR
60 70 80 90 100
DVVLMKAVGI NPVVVHGGGP QIGDLLKRLS IESHFIDGMR VTDAATMDVV
110 120 130 140 150
EMVLGGQVNK DIVNLINRHG GSAIGLTGKD AELIRAKKLT VTRQTPEMTK
160 170 180 190 200
PEIIDIGHVG EVTGVNVGLL NMLVKGDFIP VIAPIGVGSN GESYNINADL
210 220 230 240 250
VAGKVAEALK AEKLMLLTNI AGLMDKQGQV LTGLSTEQVN ELIADGTIYG
260 270 280 290 300
GMLPKIRCAL EAVQGGVTSA HIIDGRVPNA VLLEIFTDSG VGTLISNRKR

H
Length:301
Mass (Da):31,849
Last modified:January 23, 2007 - v3
Checksum:iCE0B6E912305B255
GO

Mass spectrometryi

Molecular mass is 31711 Da from positions 2 - 301. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08708.1.
PIRiA82980.
RefSeqiNP_254010.1. NC_002516.2.
WP_003096572.1. NZ_ASJY01000822.1.

Genome annotation databases

EnsemblBacteriaiAAG08708; AAG08708; PA5323.
GeneIDi879620.
KEGGipae:PA5323.
PATRICi19845503. VBIPseAer58763_5578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08708.1.
PIRiA82980.
RefSeqiNP_254010.1. NC_002516.2.
WP_003096572.1. NZ_ASJY01000822.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BUFX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L2-301[»]
ProteinModelPortaliQ9HTN2.
SMRiQ9HTN2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5323.

Chemistry databases

DrugBankiDB04075. N-Acetyl-L-Glutamate.

Proteomic databases

PaxDbiQ9HTN2.
PRIDEiQ9HTN2.

Protocols and materials databases

DNASUi879620.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08708; AAG08708; PA5323.
GeneIDi879620.
KEGGipae:PA5323.
PATRICi19845503. VBIPseAer58763_5578.

Organism-specific databases

PseudoCAPiPA5323.

Phylogenomic databases

eggNOGiENOG4105CAS. Bacteria.
COG0548. LUCA.
HOGENOMiHOG000233259.
InParanoidiQ9HTN2.
KOiK00930.
OMAiPKTECCI.
PhylomeDBiQ9HTN2.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00107.
BRENDAi2.7.2.8. 5087.

Miscellaneous databases

EvolutionaryTraceiQ9HTN2.

Family and domain databases

HAMAPiMF_00082. ArgB. 1 hit.
InterProiView protein in InterPro
IPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
PfamiView protein in Pfam
PF00696. AA_kinase. 1 hit.
PIRSFiPIRSF000728. NAGK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARGB_PSEAE
AccessioniPrimary (citable) accession number: Q9HTN2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 115 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.