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Q9V1I5 (ARGB_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetylglutamate/acetylaminoadipate kinase

EC=2.7.2.-
EC=2.7.2.8
Alternative name(s):
N-acetyl-L-glutamate/N-acetyl-L-aminoadipate 5-phosphotransferase
NAG kinase
Short name=AGK
Gene names
Name:argB
Synonyms:lysZ
Ordered Locus Names:PYRAB04420
ORF Names:PAB0292
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in both the arginine and lysine biosynthetic pathways By similarity. HAMAP MF_00082_A

Catalytic activity

ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP MF_00082_A

ATP + N-acetyl-L-aminoadipate = ADP + N-acetyl-L-aminoadipate 5-phosphate. HAMAP MF_00082_A

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP MF_00082_A

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 2/5. HAMAP MF_00082_A

Subcellular location

Cytoplasm By similarity HAMAP MF_00082_A.

Sequence similarities

Belongs to the acetylglutamate kinase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

lysine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetylglutamate kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Acetylglutamate/acetylaminoadipate kinase HAMAP MF_00082_A
PRO_0000112699

Regions

Region36 – 372Substrate binding By similarity

Sites

Binding site631Substrate By similarity
Binding site1651Substrate By similarity
Site81Transition state stabilizer By similarity
Site2211Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V1I5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7920CC2A83AF2B1D

FASTA24827,238
        10         20         30         40         50         60 
MIQMRVIKVG GSVVPMLDKI LDTSSLHGNS IIVHGGSRYV DEMARKLGVK VERLVSPSGV 

        70         80         90        100        110        120 
MFRRTTRRVL DVYVAALMRA NRELVSFLRE RGIDAIGVSG LDGVVLAKRK KLVKAVVNGK 

       130        140        150        160        170        180 
VIAIRDDYSG VIKSINVTLL KNYLKVGIPV IASIAYDPEE NVPLNVDGDK VAYHVAIAMK 

       190        200        210        220        230        240 
AKELRFLSDT AFLIDGNVVE RIPLEDFDEY LRYAGGGMKK KLMMARKALE SGVKKVVIEG 


LNGRTVIS 

« Hide

References

[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248284 Genomic DNA. Translation: CAB49364.1.
PIRE75160.
RefSeqNP_126133.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V1I5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000003833; EBPYRP00000003764; EBPYRG00000003833.
GeneID1495337.
GenomeReviewsGene locus PYRAB04420 in contig AL096836_GR.
KEGGpab:PAB0292.
NMPDRfig|272844.1.peg.461.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022350.
HOGENOMHBG497643.
OMARYTDLET.
PhylomeDBQ9V1I5.
ProtClustDBPRK14058.

Enzyme and pathway databases

BioCycPABY272844:PAB0292-MONOMER.

Family and domain databases

HAMAPMF_00082_A. ArgB_A.
[Tree]
InterProIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
KOK00930.
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000728. NAGK. 1 hit.
SUPFAMSSF53633. Aa_kinase. 1 hit.
TIGRFAMsTIGR00761. ArgB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGB_PYRAB
AccessionPrimary (citable) accession number: Q9V1I5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 2000
Last modified: December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families