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P0A6C8

- ARGB_ECOLI

UniProt

P0A6C8 - ARGB_ECOLI

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Protein
Acetylglutamate kinase
Gene
argB, b3959, JW5553
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei8 – 81Transition state stabilizer
Binding sitei66 – 661Substrate
Binding sitei158 – 1581Substrate
Sitei217 – 2171Transition state stabilizer

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1866ATPUniRule annotation
Nucleotide bindingi209 – 2113ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. acetylglutamate kinase activity Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. arginine biosynthetic process Source: EcoCyc
  2. cellular response to DNA damage stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACETYLGLUTKIN-MONOMER.
ECOL316407:JW5553-MONOMER.
MetaCyc:ACETYLGLUTKIN-MONOMER.
SABIO-RKP0A6C8.
UniPathwayiUPA00068; UER00107.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylglutamate kinase (EC:2.7.2.8)
Alternative name(s):
N-acetyl-L-glutamate 5-phosphotransferase
NAG kinase
Short name:
AGK
Gene namesi
Name:argB
Ordered Locus Names:b3959, JW5553
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10064. argB.

Subcellular locationi

Cytoplasm Inferred UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81K → R: Reduces activity 50-fold. Increases KM for N-acetyl-L-glutamate and ATP about 10-fold. 1 Publication
Mutagenesisi66 – 661R → K: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP nearly 20-fold. 1 Publication
Mutagenesisi158 – 1581N → Q: Increases KM for N-acetyl-L-glutamate over 1000-fold. Increases KM for ATP over 20-fold. 1 Publication
Mutagenesisi162 – 1621D → E: Reduces activity over 99%. No effect on KM for N-acetyl-L-glutamate and ATP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Acetylglutamate kinaseUniRule annotation
PRO_0000112614Add
BLAST

Proteomic databases

PaxDbiP0A6C8.
PRIDEiP0A6C8.

Expressioni

Gene expression databases

GenevestigatoriP0A6C8.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-9136N.
IntActiP0A6C8. 2 interactions.
MINTiMINT-1309378.
STRINGi511145.b3959.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95
Helixi11 – 155
Helixi17 – 3115
Beta strandi38 – 425
Helixi45 – 5410
Turni70 – 723
Helixi73 – 819
Helixi83 – 9412
Beta strandi99 – 1024
Helixi106 – 1083
Beta strandi110 – 1145
Turni117 – 1193
Beta strandi120 – 1278
Helixi131 – 1388
Beta strandi142 – 1509
Beta strandi156 – 1583
Helixi161 – 17212
Beta strandi175 – 18410
Helixi198 – 2069
Helixi212 – 22817
Beta strandi232 – 2387
Helixi240 – 2423
Helixi243 – 2486
Beta strandi253 – 2564

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS5X-ray1.50A1-258[»]
1GSJX-ray1.85A1-258[»]
1OH9X-ray1.91A1-258[»]
1OHAX-ray1.90A1-258[»]
1OHBX-ray1.90A1-258[»]
2WXBX-ray2.00A/B1-258[»]
2X2WX-ray2.00A/B1-258[»]
ProteinModelPortaliP0A6C8.

Miscellaneous databases

EvolutionaryTraceiP0A6C8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 452Substrate bindingUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0548.
HOGENOMiHOG000233260.
KOiK00930.
OMAiWRDAEQL.
OrthoDBiEOG6JB13D.
PhylomeDBiP0A6C8.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_00082_B. ArgB_B.
InterProiIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000728. NAGK. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6C8-1 [UniParc]FASTAAdd to Basket

« Hide

MMNPLIIKLG GVLLDSEEAL ERLFSALVNY RESHQRPLVI VHGGGCVVDE    50
LMKGLNLPVK KKNGLRVTPA DQIDIITGAL AGTANKTLLA WAKKHQIAAV 100
GLFLGDGDSV KVTQLDEELG HVGLAQPGSP KLINSLLENG YLPVVSSIGV 150
TDEGQLMNVN ADQAATALAA TLGADLILLS DVSGILDGKG QRIAEMTAAK 200
AEQLIEQGII TDGMIVKVNA ALDAARTLGR PVDIASWRHA EQLPALFNGM 250
PMGTRILA 258
Length:258
Mass (Da):27,160
Last modified:June 7, 2005 - v1
Checksum:i8B916B8CBC143738
GO

Sequence cautioni

The sequence BAE77352.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiJT0331. KIECAE.
RefSeqiNP_418394.3. NC_000913.3.
YP_491493.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76941; AAC76941; b3959.
BAE77352; BAE77352; BAE77352.
GeneIDi12932895.
948464.
KEGGiecj:Y75_p3229.
eco:b3959.
PATRICi32123439. VBIEscCol129921_4080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi JT0331. KIECAE.
RefSeqi NP_418394.3. NC_000913.3.
YP_491493.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0A6C8.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-9136N.
IntActi P0A6C8. 2 interactions.
MINTi MINT-1309378.
STRINGi 511145.b3959.

Proteomic databases

PaxDbi P0A6C8.
PRIDEi P0A6C8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76941 ; AAC76941 ; b3959 .
BAE77352 ; BAE77352 ; BAE77352 .
GeneIDi 12932895.
948464.
KEGGi ecj:Y75_p3229.
eco:b3959.
PATRICi 32123439. VBIEscCol129921_4080.

Organism-specific databases

EchoBASEi EB0062.
EcoGenei EG10064. argB.

Phylogenomic databases

eggNOGi COG0548.
HOGENOMi HOG000233260.
KOi K00930.
OMAi WRDAEQL.
OrthoDBi EOG6JB13D.
PhylomeDBi P0A6C8.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00107 .
BioCyci EcoCyc:ACETYLGLUTKIN-MONOMER.
ECOL316407:JW5553-MONOMER.
MetaCyc:ACETYLGLUTKIN-MONOMER.
SABIO-RK P0A6C8.

Miscellaneous databases

EvolutionaryTracei P0A6C8.
PROi P0A6C8.

Gene expression databases

Genevestigatori P0A6C8.

Family and domain databases

Gene3Di 3.40.1160.10. 1 hit.
HAMAPi MF_00082_B. ArgB_B.
InterProi IPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
[Graphical view ]
Pfami PF00696. AA_kinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000728. NAGK. 1 hit.
SUPFAMi SSF53633. SSF53633. 1 hit.
TIGRFAMsi TIGR00761. argB. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiARGB_ECOLI
AccessioniPrimary (citable) accession number: P0A6C8
Secondary accession number(s): P11445, Q2M8Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: June 11, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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