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A3CRT9 (ARGB_METMJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:Memar_0154
OrganismMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [Complete proteome] [HAMAP]
Taxonomic identifier368407 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP-Rule MF_00082

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP-Rule MF_00082

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00082.

Sequence similarities

Belongs to the acetylglutamate kinase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine 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-HAMAP

proline biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

acetylglutamate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate 5-kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Acetylglutamate kinase HAMAP-Rule MF_00082
PRO_1000010509

Regions

Region60 – 612Substrate binding By similarity

Sites

Binding site821Substrate By similarity
Binding site1861Substrate By similarity
Site251Transition state stabilizer By similarity
Site2471Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CRT9 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 0623127845D9795F

FASTA28930,949
        10         20         30         40         50         60 
MKREDVLMEA LPYIQKFYGK TIVIKLGGHA MVDQSILETV IRDAVLLRYV GMKVVLVHGG 

        70         80         90        100        110        120 
GPEITAKMQA MGKEPKFVGG LRITDPETLE IAQMVLVGKI NDGIVSLIAN CGTRAVGISG 

       130        140        150        160        170        180 
NDGNLLIARK MDPQRVQVGE VMQEVDLGQV GEIEEVDPEV LHCLLAQNYI PVVAPIAIDR 

       190        200        210        220        230        240 
QGMSLNINAD TAAAEIAIAL SAFKLVNLTD VDGVMDADRT MVYHRLALTE AEAMIGAGVI 

       250        260        270        280 
AGGMIPKLEG CMKAVRNGVA SAHVVNGNRE HNLLLELFTD QGVGTMLTL 

« Hide

References

[1]"Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1."
Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., Land M. expand/collapse author list , Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:189-196(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35101 / DSM 1498 / JR1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000562 Genomic DNA. Translation: ABN56089.1.
RefSeqYP_001046071.1. NC_009051.1.

3D structure databases

ProteinModelPortalA3CRT9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368407.Memar_0154.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN56089; ABN56089; Memar_0154.
GeneID4848336.
KEGGmem:Memar_0154.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0548.
HOGENOMHOG000233259.
KOK00930.
OMAFDVHTDL.

Enzyme and pathway databases

BioCycMMAR368407:GH7L-154-MONOMER.
UniPathwayUPA00068; UER00107.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
HAMAPMF_00082_A. ArgB_A.
MF_00082_B. ArgB_B.
InterProIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000728. NAGK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00761. argB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGB_METMJ
AccessionPrimary (citable) accession number: A3CRT9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways